Full text data of PPCDC
PPCDC
(COAC)
[Confidence: low (only semi-automatic identification from reviews)]
Phosphopantothenoylcysteine decarboxylase; PPC-DC; 4.1.1.36 (CoaC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphopantothenoylcysteine decarboxylase; PPC-DC; 4.1.1.36 (CoaC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96CD2
ID COAC_HUMAN Reviewed; 204 AA.
AC Q96CD2; Q96SX0; Q9HC17;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase;
DE Short=PPC-DC;
DE EC=4.1.1.36;
DE AltName: Full=CoaC;
GN Name=PPCDC; Synonyms=COAC; ORFNames=MDS018, UNQ9365/PRO34154;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION, AND FUNCTION.
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 [7]
RP FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=15581364; DOI=10.1021/bi048340a;
RA Strauss E., Zhai H., Brand L.A., McLafferty F.W., Begley T.P.;
RT "Mechanistic studies on phosphopantothenoylcysteine decarboxylase:
RT trapping of an enethiolate intermediate with a mechanism-based
RT inactivating agent.";
RL Biochemistry 43:15520-15533(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) IN COMPLEX WITH FMN.
RX PubMed=14501115; DOI=10.1107/S0907444903016214;
RA Manoj N., Ealick S.E.;
RT "Unusual space-group pseudosymmetry in crystals of human
RT phosphopantothenoylcysteine decarboxylase.";
RL Acta Crystallogr. D 59:1762-1766(2003).
CC -!- FUNCTION: Necessary for the biosynthesis of coenzyme A. Catalyzes
CC the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-
CC phosphopantotheine.
CC -!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine =
CC pantotheine 4'-phosphate + CO(2).
CC -!- COFACTOR: Binds 1 FMN per subunit.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 3/5.
CC -!- SUBUNIT: Homotrimer (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96CD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CD2-2; Sequence=VSP_044802;
CC Note=The Met-1 codon is associated with a polymorphism
CC (dbSNP:rs2304899) that replaces the initiation ATG codon by an
CC ATA codon;
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing
CC Cys decarboxylase) superfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF182419; AAG14955.1; -; mRNA.
DR EMBL; AY358848; AAQ89207.1; -; mRNA.
DR EMBL; AK027491; BAB55151.1; -; mRNA.
DR EMBL; AC015720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014409; AAH14409.1; -; mRNA.
DR RefSeq; NP_068595.3; NM_021823.3.
DR UniGene; Hs.458922; -.
DR PDB; 1QZU; X-ray; 2.91 A; A/B/C/D=1-204.
DR PDBsum; 1QZU; -.
DR ProteinModelPortal; Q96CD2; -.
DR SMR; Q96CD2; 14-194.
DR IntAct; Q96CD2; 4.
DR MINT; MINT-1394867; -.
DR STRING; 9606.ENSP00000343190; -.
DR PhosphoSite; Q96CD2; -.
DR DMDM; 296434457; -.
DR PaxDb; Q96CD2; -.
DR PRIDE; Q96CD2; -.
DR DNASU; 60490; -.
DR Ensembl; ENST00000342932; ENSP00000343190; ENSG00000138621.
DR GeneID; 60490; -.
DR KEGG; hsa:60490; -.
DR UCSC; uc002azo.3; human.
DR CTD; 60490; -.
DR GeneCards; GC15P075315; -.
DR H-InvDB; HIX0202140; -.
DR HGNC; HGNC:28107; PPCDC.
DR HPA; HPA045667; -.
DR MIM; 609854; gene.
DR neXtProt; NX_Q96CD2; -.
DR PharmGKB; PA142671157; -.
DR eggNOG; COG0452; -.
DR HOGENOM; HOG000187629; -.
DR HOVERGEN; HBG054722; -.
DR InParanoid; Q96CD2; -.
DR KO; K01598; -.
DR OMA; MEPKASC; -.
DR OrthoDB; EOG738062; -.
DR PhylomeDB; Q96CD2; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q96CD2; -.
DR UniPathway; UPA00241; UER00354.
DR EvolutionaryTrace; Q96CD2; -.
DR GenomeRNAi; 60490; -.
DR NextBio; 65379; -.
DR PRO; PR:Q96CD2; -.
DR ArrayExpress; Q96CD2; -.
DR Bgee; Q96CD2; -.
DR CleanEx; HS_PPCDC; -.
DR Genevestigator; Q96CD2; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase 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; 3.40.50.1950; -; 1.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coenzyme A biosynthesis;
KW Complete proteome; Decarboxylase; Flavoprotein; FMN; Lyase;
KW Polymorphism; Reference proteome.
FT CHAIN 1 204 Phosphopantothenoylcysteine
FT decarboxylase.
FT /FTId=PRO_0000182030.
FT NP_BIND 104 107 FMN.
FT ACT_SITE 173 173 Proton donor.
FT BINDING 59 59 FMN.
FT BINDING 140 140 Substrate (By similarity).
FT VAR_SEQ 1 78 MEPKASCPAAAPLMERKFHVLVGVTGSVAALKLPLLVSKLL
FT DIPGLEVAVVTTERAKHFYSPQDIPVTLYSDADEWEI ->
FT M (in isoform 2).
FT /FTId=VSP_044802.
FT VARIANT 78 78 I -> M (in dbSNP:rs2304899).
FT /FTId=VAR_068974.
FT CONFLICT 49 49 A -> S (in Ref. 3; BAB55151).
FT STRAND 16 24
FT HELIX 28 31
FT HELIX 33 40
FT STRAND 46 52
FT HELIX 55 58
FT HELIX 62 64
FT HELIX 72 77
FT HELIX 87 92
FT STRAND 96 103
FT HELIX 105 112
FT HELIX 119 125
FT STRAND 135 137
FT HELIX 141 144
FT HELIX 149 157
FT HELIX 186 191
SQ SEQUENCE 204 AA; 22395 MW; 9E59683480032894 CRC64;
MEPKASCPAA APLMERKFHV LVGVTGSVAA LKLPLLVSKL LDIPGLEVAV VTTERAKHFY
SPQDIPVTLY SDADEWEIWK SRSDPVLHID LRRWADLLLV APLDANTLGK VASGICDNLL
TCVMRAWDRS KPLLFCPAMN TAMWEHPITA QQVDQLKAFG YVEIPCVAKK LVCGDEGLGA
MAEVGTIVDK VKEVLFQHSG FQQS
//
ID COAC_HUMAN Reviewed; 204 AA.
AC Q96CD2; Q96SX0; Q9HC17;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase;
DE Short=PPC-DC;
DE EC=4.1.1.36;
DE AltName: Full=CoaC;
GN Name=PPCDC; Synonyms=COAC; ORFNames=MDS018, UNQ9365/PRO34154;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION, AND FUNCTION.
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 [7]
RP FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=15581364; DOI=10.1021/bi048340a;
RA Strauss E., Zhai H., Brand L.A., McLafferty F.W., Begley T.P.;
RT "Mechanistic studies on phosphopantothenoylcysteine decarboxylase:
RT trapping of an enethiolate intermediate with a mechanism-based
RT inactivating agent.";
RL Biochemistry 43:15520-15533(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) IN COMPLEX WITH FMN.
RX PubMed=14501115; DOI=10.1107/S0907444903016214;
RA Manoj N., Ealick S.E.;
RT "Unusual space-group pseudosymmetry in crystals of human
RT phosphopantothenoylcysteine decarboxylase.";
RL Acta Crystallogr. D 59:1762-1766(2003).
CC -!- FUNCTION: Necessary for the biosynthesis of coenzyme A. Catalyzes
CC the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-
CC phosphopantotheine.
CC -!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine =
CC pantotheine 4'-phosphate + CO(2).
CC -!- COFACTOR: Binds 1 FMN per subunit.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 3/5.
CC -!- SUBUNIT: Homotrimer (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96CD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CD2-2; Sequence=VSP_044802;
CC Note=The Met-1 codon is associated with a polymorphism
CC (dbSNP:rs2304899) that replaces the initiation ATG codon by an
CC ATA codon;
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing
CC Cys decarboxylase) superfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF182419; AAG14955.1; -; mRNA.
DR EMBL; AY358848; AAQ89207.1; -; mRNA.
DR EMBL; AK027491; BAB55151.1; -; mRNA.
DR EMBL; AC015720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014409; AAH14409.1; -; mRNA.
DR RefSeq; NP_068595.3; NM_021823.3.
DR UniGene; Hs.458922; -.
DR PDB; 1QZU; X-ray; 2.91 A; A/B/C/D=1-204.
DR PDBsum; 1QZU; -.
DR ProteinModelPortal; Q96CD2; -.
DR SMR; Q96CD2; 14-194.
DR IntAct; Q96CD2; 4.
DR MINT; MINT-1394867; -.
DR STRING; 9606.ENSP00000343190; -.
DR PhosphoSite; Q96CD2; -.
DR DMDM; 296434457; -.
DR PaxDb; Q96CD2; -.
DR PRIDE; Q96CD2; -.
DR DNASU; 60490; -.
DR Ensembl; ENST00000342932; ENSP00000343190; ENSG00000138621.
DR GeneID; 60490; -.
DR KEGG; hsa:60490; -.
DR UCSC; uc002azo.3; human.
DR CTD; 60490; -.
DR GeneCards; GC15P075315; -.
DR H-InvDB; HIX0202140; -.
DR HGNC; HGNC:28107; PPCDC.
DR HPA; HPA045667; -.
DR MIM; 609854; gene.
DR neXtProt; NX_Q96CD2; -.
DR PharmGKB; PA142671157; -.
DR eggNOG; COG0452; -.
DR HOGENOM; HOG000187629; -.
DR HOVERGEN; HBG054722; -.
DR InParanoid; Q96CD2; -.
DR KO; K01598; -.
DR OMA; MEPKASC; -.
DR OrthoDB; EOG738062; -.
DR PhylomeDB; Q96CD2; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q96CD2; -.
DR UniPathway; UPA00241; UER00354.
DR EvolutionaryTrace; Q96CD2; -.
DR GenomeRNAi; 60490; -.
DR NextBio; 65379; -.
DR PRO; PR:Q96CD2; -.
DR ArrayExpress; Q96CD2; -.
DR Bgee; Q96CD2; -.
DR CleanEx; HS_PPCDC; -.
DR Genevestigator; Q96CD2; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase 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; 3.40.50.1950; -; 1.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coenzyme A biosynthesis;
KW Complete proteome; Decarboxylase; Flavoprotein; FMN; Lyase;
KW Polymorphism; Reference proteome.
FT CHAIN 1 204 Phosphopantothenoylcysteine
FT decarboxylase.
FT /FTId=PRO_0000182030.
FT NP_BIND 104 107 FMN.
FT ACT_SITE 173 173 Proton donor.
FT BINDING 59 59 FMN.
FT BINDING 140 140 Substrate (By similarity).
FT VAR_SEQ 1 78 MEPKASCPAAAPLMERKFHVLVGVTGSVAALKLPLLVSKLL
FT DIPGLEVAVVTTERAKHFYSPQDIPVTLYSDADEWEI ->
FT M (in isoform 2).
FT /FTId=VSP_044802.
FT VARIANT 78 78 I -> M (in dbSNP:rs2304899).
FT /FTId=VAR_068974.
FT CONFLICT 49 49 A -> S (in Ref. 3; BAB55151).
FT STRAND 16 24
FT HELIX 28 31
FT HELIX 33 40
FT STRAND 46 52
FT HELIX 55 58
FT HELIX 62 64
FT HELIX 72 77
FT HELIX 87 92
FT STRAND 96 103
FT HELIX 105 112
FT HELIX 119 125
FT STRAND 135 137
FT HELIX 141 144
FT HELIX 149 157
FT HELIX 186 191
SQ SEQUENCE 204 AA; 22395 MW; 9E59683480032894 CRC64;
MEPKASCPAA APLMERKFHV LVGVTGSVAA LKLPLLVSKL LDIPGLEVAV VTTERAKHFY
SPQDIPVTLY SDADEWEIWK SRSDPVLHID LRRWADLLLV APLDANTLGK VASGICDNLL
TCVMRAWDRS KPLLFCPAMN TAMWEHPITA QQVDQLKAFG YVEIPCVAKK LVCGDEGLGA
MAEVGTIVDK VKEVLFQHSG FQQS
//
MIM
609854
*RECORD*
*FIELD* NO
609854
*FIELD* TI
*609854 PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE; PPCDC
*FIELD* TX
DESCRIPTION
Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is
read morean essential universal pathway in prokaryotes and eukaryotes. PPCDC (EC
4.1.1.36), one of the last enzymes in this pathway, converts
phosphopantothenoylcysteine to 4-prime-phosphopantetheine (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
human PPCDC.
GENE FUNCTION
Daugherty et al. (2002) showed that recombinant PPCDC functioned within
the CoA synthetic pathway, and they verified PPCDC function by
complementation in E. coli. Incubation of PPCS (609853), PPCDC, and the
bifunctional enzyme COASY (609855) with the necessary substrates and
cofactors reconstituted the 4-step biochemical transformation of
phosphopantothenate to CoA.
MAPPING
By genomic sequence analysis, Daugherty et al. (2002) mapped the PPCDC
gene to chromosome 15.
*FIELD* RF
1. 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.
*FIELD* CD
Patricia A. Hartz: 1/27/2006
*FIELD* ED
mgross: 01/27/2006
*RECORD*
*FIELD* NO
609854
*FIELD* TI
*609854 PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE; PPCDC
*FIELD* TX
DESCRIPTION
Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is
read morean essential universal pathway in prokaryotes and eukaryotes. PPCDC (EC
4.1.1.36), one of the last enzymes in this pathway, converts
phosphopantothenoylcysteine to 4-prime-phosphopantetheine (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
human PPCDC.
GENE FUNCTION
Daugherty et al. (2002) showed that recombinant PPCDC functioned within
the CoA synthetic pathway, and they verified PPCDC function by
complementation in E. coli. Incubation of PPCS (609853), PPCDC, and the
bifunctional enzyme COASY (609855) with the necessary substrates and
cofactors reconstituted the 4-step biochemical transformation of
phosphopantothenate to CoA.
MAPPING
By genomic sequence analysis, Daugherty et al. (2002) mapped the PPCDC
gene to chromosome 15.
*FIELD* RF
1. 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.
*FIELD* CD
Patricia A. Hartz: 1/27/2006
*FIELD* ED
mgross: 01/27/2006