Full text data of COASY
COASY
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Bifunctional coenzyme A synthase; CoA synthase (NBP; POV-2; Phosphopantetheine adenylyltransferase; 2.7.7.3; Dephospho-CoA pyrophosphorylase; Pantetheine-phosphate adenylyltransferase; PPAT; Dephospho-CoA kinase; DPCK; 2.7.1.24; Dephosphocoenzyme A kinase; DPCOAK)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Bifunctional coenzyme A synthase; CoA synthase (NBP; POV-2; Phosphopantetheine adenylyltransferase; 2.7.7.3; Dephospho-CoA pyrophosphorylase; Pantetheine-phosphate adenylyltransferase; PPAT; Dephospho-CoA kinase; DPCK; 2.7.1.24; Dephosphocoenzyme A kinase; DPCOAK)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00184821
IPI00184821 Bifunctional coenzyme A synthase Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway, May act as a point of CoA biosynthesis regulation. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00184821 Bifunctional coenzyme A synthase Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway, May act as a point of CoA biosynthesis regulation. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q13057
ID COASY_HUMAN Reviewed; 564 AA.
AC Q13057; B2RA78; B4DLU0; Q6GS23; Q8NBM7; Q8NEW1; Q8WXD4; Q9NRM3;
read moreDT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 4.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=Bifunctional coenzyme A synthase;
DE Short=CoA synthase;
DE AltName: Full=NBP;
DE AltName: Full=POV-2;
DE Includes:
DE RecName: Full=Phosphopantetheine adenylyltransferase;
DE EC=2.7.7.3;
DE AltName: Full=Dephospho-CoA pyrophosphorylase;
DE AltName: Full=Pantetheine-phosphate adenylyltransferase;
DE Short=PPAT;
DE Includes:
DE RecName: Full=Dephospho-CoA kinase;
DE Short=DPCK;
DE EC=2.7.1.24;
DE AltName: Full=Dephosphocoenzyme A kinase;
DE Short=DPCOAK;
GN Name=COASY; ORFNames=PSEC0106;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP AND VARIANT TYR-55.
RX PubMed=11923312; DOI=10.1074/jbc.M201708200;
RA Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A.,
RA de Crecy-Lagard V., Osterman A.;
RT "Complete reconstitution of the human coenzyme A biosynthetic pathway
RT via comparative genomics.";
RL J. Biol. Chem. 277:21431-21439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RX PubMed=11994049; DOI=10.1042/BJ20020569;
RA Aghajanian S., Worrall D.M.;
RT "Identification and characterization of the gene encoding the human
RT phosphopantetheine adenylyltransferase and dephospho-CoA kinase
RT bifunctional enzyme (CoA synthase).";
RL Biochem. J. 365:13-18(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RA Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S.,
RA Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y.,
RA Nagahari K., Sugano S., Isogai T.;
RT "HRI human cDNA sequencing project.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TYR-55.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-55.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP TYR-55.
RC TISSUE=Colon, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-564 (ISOFORMS 1/2).
RA Zhu Y.-B., Han Y.;
RT "Molecular cloning of a NBP gene cDNA.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-564 (ISOFORMS 1/2).
RC TISSUE=Ovary;
RX PubMed=8529999; DOI=10.1007/BF00197407;
RA Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.;
RT "A 100-kb physical and transcriptional map around the EDH17B2 gene:
RT identification of three novel genes and a pseudogene of a human
RT homologue of the rat PRL-1 tyrosine phosphatase.";
RL Hum. Genet. 96:532-538(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-564 (ISOFORMS 1/2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP ALTERNATIVE SPLICING.
RX PubMed=16460672; DOI=10.1016/j.bbrc.2006.01.051;
RA Nemazanyy I., Panasyuk G., Breus O., Zhyvoloup A., Filonenko V.,
RA Gout I.T.;
RT "Identification of a novel CoA synthase isoform, which is primarily
RT expressed in the brain.";
RL Biochem. Biophys. Res. Commun. 341:995-1000(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-183, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth
CC sequential steps of CoA biosynthetic pathway. The fourth reaction
CC is catalyzed by the phosphopantetheine adenylyltransferase, coded
CC by the coaD domain; the fifth reaction is catalyzed by the
CC dephospho-CoA kinase, coded by the coaE domain. May act as a point
CC of CoA biosynthesis regulation.
CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate +
CC 3'-dephospho-CoA.
CC -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 mM for 4'-phoshopantetheine;
CC KM=145 mM for ATP (in the PPAT reaction);
CC KM=16.7 mM for dephospho-CoA;
CC KM=34.4 mM for ATP (in the DPCK reaction);
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 4/5.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 5/5.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC Q6P2E9:EDC4; NbExp=3; IntAct=EBI-745967, EBI-1006038;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CoASy alpha;
CC IsoId=Q13057-1; Sequence=Displayed;
CC Name=2; Synonyms=CoASy beta;
CC IsoId=Q13057-2; Sequence=VSP_036404;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC brain, heart, skeletal muscle, colon, thymus, spleen, kidney,
CC liver, small intestine, placenta, lung and peripheral blood
CC leukocyte. Lowest expression in peripheral blood leukocytes and
CC highest in kidney and liver. Isoform 2 is expressed mainly in the
CC brain.
CC -!- SIMILARITY: In the central section; belongs to the eukaryotic CoaD
CC family.
CC -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69699.1; Type=Frameshift; Positions=535;
CC Sequence=AAF87955.1; Type=Erroneous initiation;
CC Sequence=AAH06354.1; Type=Erroneous initiation;
CC Sequence=AAH20985.1; Type=Erroneous initiation;
CC Sequence=AK075415; Type=Frameshift; Positions=315;
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DR EMBL; AF453478; AAL50813.1; -; mRNA.
DR EMBL; AY094602; AAM19996.1; -; mRNA.
DR EMBL; AK075415; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK297153; BAG59652.1; -; mRNA.
DR EMBL; AK314076; BAG36775.1; -; mRNA.
DR EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60840.1; -; Genomic_DNA.
DR EMBL; BC006354; AAH06354.1; ALT_INIT; mRNA.
DR EMBL; BC020985; AAH20985.1; ALT_INIT; mRNA.
DR EMBL; BC067254; AAH67254.1; -; mRNA.
DR EMBL; AF208536; AAF87955.1; ALT_INIT; mRNA.
DR EMBL; U18919; AAA69699.1; ALT_FRAME; mRNA.
DR EMBL; BT007168; AAP35832.1; -; mRNA.
DR RefSeq; NP_001035994.1; NM_001042529.2.
DR RefSeq; NP_001035997.2; NM_001042532.3.
DR RefSeq; NP_079509.5; NM_025233.6.
DR RefSeq; XP_005257759.1; XM_005257702.1.
DR UniGene; Hs.296422; -.
DR UniGene; Hs.742262; -.
DR ProteinModelPortal; Q13057; -.
DR SMR; Q13057; 195-557.
DR IntAct; Q13057; 3.
DR MINT; MINT-1212728; -.
DR STRING; 9606.ENSP00000377404; -.
DR PhosphoSite; Q13057; -.
DR DMDM; 32363505; -.
DR PaxDb; Q13057; -.
DR PRIDE; Q13057; -.
DR DNASU; 80347; -.
DR Ensembl; ENST00000393818; ENSP00000377406; ENSG00000068120.
DR Ensembl; ENST00000420359; ENSP00000413338; ENSG00000068120.
DR Ensembl; ENST00000421097; ENSP00000393564; ENSG00000068120.
DR Ensembl; ENST00000449624; ENSP00000407740; ENSG00000068120.
DR Ensembl; ENST00000590958; ENSP00000464814; ENSG00000068120.
DR GeneID; 80347; -.
DR KEGG; hsa:80347; -.
DR UCSC; uc002hzz.4; human.
DR CTD; 80347; -.
DR GeneCards; GC17P040714; -.
DR HGNC; HGNC:29932; COASY.
DR HPA; HPA022875; -.
DR HPA; HPA022912; -.
DR HPA; HPA023273; -.
DR MIM; 609855; gene.
DR neXtProt; NX_Q13057; -.
DR PharmGKB; PA134867942; -.
DR eggNOG; COG0237; -.
DR HOVERGEN; HBG051059; -.
DR InParanoid; Q13057; -.
DR KO; K02318; -.
DR OMA; MSGQQLV; -.
DR OrthoDB; EOG7NKKKK; -.
DR PhylomeDB; Q13057; -.
DR BRENDA; 2.7.1.24; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q13057; -.
DR UniPathway; UPA00241; UER00355.
DR UniPathway; UPA00241; UER00356.
DR ChiTaRS; COASY; human.
DR GeneWiki; COASY; -.
DR GenomeRNAi; 80347; -.
DR NextBio; 70944; -.
DR PRO; PR:Q13057; -.
DR ArrayExpress; Q13057; -.
DR Bgee; Q13057; -.
DR CleanEx; HS_COASY; -.
DR Genevestigator; Q13057; -.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:UniProtKB.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF01467; CTP_transf_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coenzyme A biosynthesis;
KW Complete proteome; Cytoplasm; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Polymorphism; Reference proteome; Transferase.
FT CHAIN 1 564 Bifunctional coenzyme A synthase.
FT /FTId=PRO_0000173039.
FT DOMAIN 360 563 DPCK.
FT NP_BIND 365 372 ATP (Potential).
FT REGION 180 358 Phosphopantetheine adenylyltransferase.
FT MOD_RES 178 178 Phosphoserine.
FT MOD_RES 183 183 Phosphoserine.
FT VAR_SEQ 1 1 M -> MRTPRLRAQPRGAVYQAPSPPPAPVGLGSM (in
FT isoform 2).
FT /FTId=VSP_036404.
FT VARIANT 55 55 S -> Y (in dbSNP:rs615942).
FT /FTId=VAR_030299.
FT CONFLICT 41 41 L -> P (in Ref. 4; BAG36775).
SQ SEQUENCE 564 AA; 62329 MW; 7DC9E93B356C5DB7 CRC64;
MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP AQPQSSPVQA
TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL PTSVQNLAHP PEVVLTDFQT
LDGSQYNPVK QQLVRYATSC YSCCPRLASV LLYSDYGIGE VPVEPLDVPL PSTIRPASPV
AGSPKQPVRG YYRGAVGGTF DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL
LQPYTERVEH LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR
FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE RPELPTCLYV
IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG PAYQPVVEAF GTDILHKDGI
INRKVLGSRV FGNKKQLKIL TDIMWPIIAK LAREEMDRAV AEGKRVCVID AAVLLEAGWQ
NLVHEVWTAV IPETEAVRRI VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI
TQRQVEKAWA LLQKRIPKTH QALD
//
ID COASY_HUMAN Reviewed; 564 AA.
AC Q13057; B2RA78; B4DLU0; Q6GS23; Q8NBM7; Q8NEW1; Q8WXD4; Q9NRM3;
read moreDT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 4.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=Bifunctional coenzyme A synthase;
DE Short=CoA synthase;
DE AltName: Full=NBP;
DE AltName: Full=POV-2;
DE Includes:
DE RecName: Full=Phosphopantetheine adenylyltransferase;
DE EC=2.7.7.3;
DE AltName: Full=Dephospho-CoA pyrophosphorylase;
DE AltName: Full=Pantetheine-phosphate adenylyltransferase;
DE Short=PPAT;
DE Includes:
DE RecName: Full=Dephospho-CoA kinase;
DE Short=DPCK;
DE EC=2.7.1.24;
DE AltName: Full=Dephosphocoenzyme A kinase;
DE Short=DPCOAK;
GN Name=COASY; ORFNames=PSEC0106;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP AND VARIANT TYR-55.
RX PubMed=11923312; DOI=10.1074/jbc.M201708200;
RA Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A.,
RA de Crecy-Lagard V., Osterman A.;
RT "Complete reconstitution of the human coenzyme A biosynthetic pathway
RT via comparative genomics.";
RL J. Biol. Chem. 277:21431-21439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RX PubMed=11994049; DOI=10.1042/BJ20020569;
RA Aghajanian S., Worrall D.M.;
RT "Identification and characterization of the gene encoding the human
RT phosphopantetheine adenylyltransferase and dephospho-CoA kinase
RT bifunctional enzyme (CoA synthase).";
RL Biochem. J. 365:13-18(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RA Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S.,
RA Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y.,
RA Nagahari K., Sugano S., Isogai T.;
RT "HRI human cDNA sequencing project.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TYR-55.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-55.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP TYR-55.
RC TISSUE=Colon, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-564 (ISOFORMS 1/2).
RA Zhu Y.-B., Han Y.;
RT "Molecular cloning of a NBP gene cDNA.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-564 (ISOFORMS 1/2).
RC TISSUE=Ovary;
RX PubMed=8529999; DOI=10.1007/BF00197407;
RA Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.;
RT "A 100-kb physical and transcriptional map around the EDH17B2 gene:
RT identification of three novel genes and a pseudogene of a human
RT homologue of the rat PRL-1 tyrosine phosphatase.";
RL Hum. Genet. 96:532-538(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-564 (ISOFORMS 1/2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP ALTERNATIVE SPLICING.
RX PubMed=16460672; DOI=10.1016/j.bbrc.2006.01.051;
RA Nemazanyy I., Panasyuk G., Breus O., Zhyvoloup A., Filonenko V.,
RA Gout I.T.;
RT "Identification of a novel CoA synthase isoform, which is primarily
RT expressed in the brain.";
RL Biochem. Biophys. Res. Commun. 341:995-1000(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-183, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth
CC sequential steps of CoA biosynthetic pathway. The fourth reaction
CC is catalyzed by the phosphopantetheine adenylyltransferase, coded
CC by the coaD domain; the fifth reaction is catalyzed by the
CC dephospho-CoA kinase, coded by the coaE domain. May act as a point
CC of CoA biosynthesis regulation.
CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate +
CC 3'-dephospho-CoA.
CC -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 mM for 4'-phoshopantetheine;
CC KM=145 mM for ATP (in the PPAT reaction);
CC KM=16.7 mM for dephospho-CoA;
CC KM=34.4 mM for ATP (in the DPCK reaction);
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 4/5.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 5/5.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC Q6P2E9:EDC4; NbExp=3; IntAct=EBI-745967, EBI-1006038;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CoASy alpha;
CC IsoId=Q13057-1; Sequence=Displayed;
CC Name=2; Synonyms=CoASy beta;
CC IsoId=Q13057-2; Sequence=VSP_036404;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC brain, heart, skeletal muscle, colon, thymus, spleen, kidney,
CC liver, small intestine, placenta, lung and peripheral blood
CC leukocyte. Lowest expression in peripheral blood leukocytes and
CC highest in kidney and liver. Isoform 2 is expressed mainly in the
CC brain.
CC -!- SIMILARITY: In the central section; belongs to the eukaryotic CoaD
CC family.
CC -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69699.1; Type=Frameshift; Positions=535;
CC Sequence=AAF87955.1; Type=Erroneous initiation;
CC Sequence=AAH06354.1; Type=Erroneous initiation;
CC Sequence=AAH20985.1; Type=Erroneous initiation;
CC Sequence=AK075415; Type=Frameshift; Positions=315;
CC -----------------------------------------------------------------------
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DR EMBL; AF453478; AAL50813.1; -; mRNA.
DR EMBL; AY094602; AAM19996.1; -; mRNA.
DR EMBL; AK075415; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK297153; BAG59652.1; -; mRNA.
DR EMBL; AK314076; BAG36775.1; -; mRNA.
DR EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60840.1; -; Genomic_DNA.
DR EMBL; BC006354; AAH06354.1; ALT_INIT; mRNA.
DR EMBL; BC020985; AAH20985.1; ALT_INIT; mRNA.
DR EMBL; BC067254; AAH67254.1; -; mRNA.
DR EMBL; AF208536; AAF87955.1; ALT_INIT; mRNA.
DR EMBL; U18919; AAA69699.1; ALT_FRAME; mRNA.
DR EMBL; BT007168; AAP35832.1; -; mRNA.
DR RefSeq; NP_001035994.1; NM_001042529.2.
DR RefSeq; NP_001035997.2; NM_001042532.3.
DR RefSeq; NP_079509.5; NM_025233.6.
DR RefSeq; XP_005257759.1; XM_005257702.1.
DR UniGene; Hs.296422; -.
DR UniGene; Hs.742262; -.
DR ProteinModelPortal; Q13057; -.
DR SMR; Q13057; 195-557.
DR IntAct; Q13057; 3.
DR MINT; MINT-1212728; -.
DR STRING; 9606.ENSP00000377404; -.
DR PhosphoSite; Q13057; -.
DR DMDM; 32363505; -.
DR PaxDb; Q13057; -.
DR PRIDE; Q13057; -.
DR DNASU; 80347; -.
DR Ensembl; ENST00000393818; ENSP00000377406; ENSG00000068120.
DR Ensembl; ENST00000420359; ENSP00000413338; ENSG00000068120.
DR Ensembl; ENST00000421097; ENSP00000393564; ENSG00000068120.
DR Ensembl; ENST00000449624; ENSP00000407740; ENSG00000068120.
DR Ensembl; ENST00000590958; ENSP00000464814; ENSG00000068120.
DR GeneID; 80347; -.
DR KEGG; hsa:80347; -.
DR UCSC; uc002hzz.4; human.
DR CTD; 80347; -.
DR GeneCards; GC17P040714; -.
DR HGNC; HGNC:29932; COASY.
DR HPA; HPA022875; -.
DR HPA; HPA022912; -.
DR HPA; HPA023273; -.
DR MIM; 609855; gene.
DR neXtProt; NX_Q13057; -.
DR PharmGKB; PA134867942; -.
DR eggNOG; COG0237; -.
DR HOVERGEN; HBG051059; -.
DR InParanoid; Q13057; -.
DR KO; K02318; -.
DR OMA; MSGQQLV; -.
DR OrthoDB; EOG7NKKKK; -.
DR PhylomeDB; Q13057; -.
DR BRENDA; 2.7.1.24; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q13057; -.
DR UniPathway; UPA00241; UER00355.
DR UniPathway; UPA00241; UER00356.
DR ChiTaRS; COASY; human.
DR GeneWiki; COASY; -.
DR GenomeRNAi; 80347; -.
DR NextBio; 70944; -.
DR PRO; PR:Q13057; -.
DR ArrayExpress; Q13057; -.
DR Bgee; Q13057; -.
DR CleanEx; HS_COASY; -.
DR Genevestigator; Q13057; -.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:UniProtKB.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF01467; CTP_transf_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coenzyme A biosynthesis;
KW Complete proteome; Cytoplasm; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Polymorphism; Reference proteome; Transferase.
FT CHAIN 1 564 Bifunctional coenzyme A synthase.
FT /FTId=PRO_0000173039.
FT DOMAIN 360 563 DPCK.
FT NP_BIND 365 372 ATP (Potential).
FT REGION 180 358 Phosphopantetheine adenylyltransferase.
FT MOD_RES 178 178 Phosphoserine.
FT MOD_RES 183 183 Phosphoserine.
FT VAR_SEQ 1 1 M -> MRTPRLRAQPRGAVYQAPSPPPAPVGLGSM (in
FT isoform 2).
FT /FTId=VSP_036404.
FT VARIANT 55 55 S -> Y (in dbSNP:rs615942).
FT /FTId=VAR_030299.
FT CONFLICT 41 41 L -> P (in Ref. 4; BAG36775).
SQ SEQUENCE 564 AA; 62329 MW; 7DC9E93B356C5DB7 CRC64;
MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP AQPQSSPVQA
TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL PTSVQNLAHP PEVVLTDFQT
LDGSQYNPVK QQLVRYATSC YSCCPRLASV LLYSDYGIGE VPVEPLDVPL PSTIRPASPV
AGSPKQPVRG YYRGAVGGTF DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL
LQPYTERVEH LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR
FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE RPELPTCLYV
IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG PAYQPVVEAF GTDILHKDGI
INRKVLGSRV FGNKKQLKIL TDIMWPIIAK LAREEMDRAV AEGKRVCVID AAVLLEAGWQ
NLVHEVWTAV IPETEAVRRI VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI
TQRQVEKAWA LLQKRIPKTH QALD
//
MIM
609855
*RECORD*
*FIELD* NO
609855
*FIELD* TI
*609855 COENZYME A SYNTHASE; COASY
;;PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE/DEPHOSPHOCOENZYME A KINASE;;
read morePPAT/DPCK
*FIELD* TX
DESCRIPTION
Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is
an essential universal pathway in prokaryotes and eukaryotes. COASY is a
bifunctional enzyme that catalyzes the 2 last steps in CoA synthesis.
These activities are performed by 2 separate enzymes, phosphopantetheine
adenylyltransferase (PPAT; EC 2.7.7.3) and dephospho-CoA kinase (DPCK;
EC 2.7.1.24), in prokaryotes (Daugherty et al., 2002).
CLONING
By searching for sequences similar to E. coli CoA biosynthesis enzymes,
followed by PCR of a brain cDNA library, Daugherty et al. (2002) cloned
COASY, which they called PPAT/DPCK. The deduced 565-amino acid protein
has an N-terminal domain, a central PPAT domain, and a C-terminal DPCK
domain. The PPAT domain contains the conserved HxxH motif characteristic
of nucleotidyltransferases. Northern blot analysis detected 2.2- and
2.6-kb COASY transcripts in most tissues and tumor cell lines examined.
Expression was highest in kidney and liver and lowest in peripheral
blood leukocytes.
By searching for sequences similar to pig Coasy, followed by RT-PCR of a
hepatoma cell line cDNA library, Aghajanian and Worrall (2002) cloned
human COASY. The deduced protein has a calculated molecular mass of 62.3
kD and shares more than 96% amino acid identity with the pig and mouse
proteins. Aghajanian and Worrall (2002) identified a conserved Walker
A-type kinase motif, which is involved in ATP binding, in the C-terminal
DPCK domain of COASY. Size-exclusion chromatography showed that
recombinant human COASY assumed a monomeric native structure with an
apparent molecular mass of 62 kD.
Using full-length ribosomal S6 kinase alpha-II (RPS6KA2; 601685) as bait
in a yeast 2-hybrid screen of a mouse embryo cDNA library, Zhyvoloup et
al. (2002) cloned mouse Coasy, which encodes a deduced 563-amino acid
protein. Bioinformatic analysis indicated that the N-terminal extension
is only present in eukaryotes.
GENE FUNCTION
Daugherty et al. (2002) showed that recombinant COASY functioned as the
last enzyme within the CoA synthetic pathway, and they verified COASY
function by complementation in E. coli. Incubation of PPCS (609853),
PPCDC (609854), and COASY with the necessary substrates and cofactors
reconstituted the 4-step biochemical transformation of
phosphopantothenate to CoA. Mutation analysis confirmed the bifunctional
activity of COASY.
Zhyvoloup et al. (2002) confirmed that mouse Coasy is a bifunctional
enzyme. Mutation of his203 to ala in the catalytic pocket of the PPAT
domain inactivated PPAT activity.
GENE STRUCTURE
Aghajanian and Worrall (2002) determined that the COASY gene contains 10
exons.
MAPPING
By genomic sequence analysis, Aghajanian and Worrall (2002) mapped the
COASY gene to chromosome 17q12-q21.
*FIELD* RF
1. Aghajanian, S.; Worrall, D. M.: Identification and characterization
of the gene encoding the human phosphopantetheine adenylyltransferase
and dephospho-CoA kinase bifunctional enzyme (CoA synthase). Biochem.
J. 365: 13-18, 2002.
2. Daugherty, M.; Polanuyer, B.; Farrell, M.; Scholle, M.; Lykidis,
A.; de Crecy-Lagard, V.; Osterman, A.: Complete reconstitution of
the human coenzyme A biosynthetic pathway via comparative genomics. J.
Biol. Chem. 277: 21431-21439, 2002.
3. Zhyvoloup, A.; Nemazanyy, I.; Babich, A.; Panasyuk, G.; Pobigailo,
N.; Vudmaska, M.; Naidenov, V.; Kukharenko, O.; Palchevskii, S.; Savinska,
L.; Ovcharenko, G.; Verdier, F.; Valovka, T.; Fenton, T.; Rebholz,
H.; Wang, M.-L.; Shepherd, P.; Matsuka, G.; Filonenko, V.; Gout, I.
T.: Molecular cloning of CoA synthase: the missing link in CoA biosynthesis. J.
Biol. Chem. 277: 22107-22110, 2002.
*FIELD* CD
Patricia A. Hartz: 1/27/2006
*FIELD* ED
mgross: 01/27/2006
*RECORD*
*FIELD* NO
609855
*FIELD* TI
*609855 COENZYME A SYNTHASE; COASY
;;PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE/DEPHOSPHOCOENZYME A KINASE;;
read morePPAT/DPCK
*FIELD* TX
DESCRIPTION
Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is
an essential universal pathway in prokaryotes and eukaryotes. COASY is a
bifunctional enzyme that catalyzes the 2 last steps in CoA synthesis.
These activities are performed by 2 separate enzymes, phosphopantetheine
adenylyltransferase (PPAT; EC 2.7.7.3) and dephospho-CoA kinase (DPCK;
EC 2.7.1.24), in prokaryotes (Daugherty et al., 2002).
CLONING
By searching for sequences similar to E. coli CoA biosynthesis enzymes,
followed by PCR of a brain cDNA library, Daugherty et al. (2002) cloned
COASY, which they called PPAT/DPCK. The deduced 565-amino acid protein
has an N-terminal domain, a central PPAT domain, and a C-terminal DPCK
domain. The PPAT domain contains the conserved HxxH motif characteristic
of nucleotidyltransferases. Northern blot analysis detected 2.2- and
2.6-kb COASY transcripts in most tissues and tumor cell lines examined.
Expression was highest in kidney and liver and lowest in peripheral
blood leukocytes.
By searching for sequences similar to pig Coasy, followed by RT-PCR of a
hepatoma cell line cDNA library, Aghajanian and Worrall (2002) cloned
human COASY. The deduced protein has a calculated molecular mass of 62.3
kD and shares more than 96% amino acid identity with the pig and mouse
proteins. Aghajanian and Worrall (2002) identified a conserved Walker
A-type kinase motif, which is involved in ATP binding, in the C-terminal
DPCK domain of COASY. Size-exclusion chromatography showed that
recombinant human COASY assumed a monomeric native structure with an
apparent molecular mass of 62 kD.
Using full-length ribosomal S6 kinase alpha-II (RPS6KA2; 601685) as bait
in a yeast 2-hybrid screen of a mouse embryo cDNA library, Zhyvoloup et
al. (2002) cloned mouse Coasy, which encodes a deduced 563-amino acid
protein. Bioinformatic analysis indicated that the N-terminal extension
is only present in eukaryotes.
GENE FUNCTION
Daugherty et al. (2002) showed that recombinant COASY functioned as the
last enzyme within the CoA synthetic pathway, and they verified COASY
function by complementation in E. coli. Incubation of PPCS (609853),
PPCDC (609854), and COASY with the necessary substrates and cofactors
reconstituted the 4-step biochemical transformation of
phosphopantothenate to CoA. Mutation analysis confirmed the bifunctional
activity of COASY.
Zhyvoloup et al. (2002) confirmed that mouse Coasy is a bifunctional
enzyme. Mutation of his203 to ala in the catalytic pocket of the PPAT
domain inactivated PPAT activity.
GENE STRUCTURE
Aghajanian and Worrall (2002) determined that the COASY gene contains 10
exons.
MAPPING
By genomic sequence analysis, Aghajanian and Worrall (2002) mapped the
COASY gene to chromosome 17q12-q21.
*FIELD* RF
1. Aghajanian, S.; Worrall, D. M.: Identification and characterization
of the gene encoding the human phosphopantetheine adenylyltransferase
and dephospho-CoA kinase bifunctional enzyme (CoA synthase). Biochem.
J. 365: 13-18, 2002.
2. Daugherty, M.; Polanuyer, B.; Farrell, M.; Scholle, M.; Lykidis,
A.; de Crecy-Lagard, V.; Osterman, A.: Complete reconstitution of
the human coenzyme A biosynthetic pathway via comparative genomics. J.
Biol. Chem. 277: 21431-21439, 2002.
3. Zhyvoloup, A.; Nemazanyy, I.; Babich, A.; Panasyuk, G.; Pobigailo,
N.; Vudmaska, M.; Naidenov, V.; Kukharenko, O.; Palchevskii, S.; Savinska,
L.; Ovcharenko, G.; Verdier, F.; Valovka, T.; Fenton, T.; Rebholz,
H.; Wang, M.-L.; Shepherd, P.; Matsuka, G.; Filonenko, V.; Gout, I.
T.: Molecular cloning of CoA synthase: the missing link in CoA biosynthesis. J.
Biol. Chem. 277: 22107-22110, 2002.
*FIELD* CD
Patricia A. Hartz: 1/27/2006
*FIELD* ED
mgross: 01/27/2006