Full text data of NADSYN1
NADSYN1
[Confidence: low (only semi-automatic identification from reviews)]
Glutamine-dependent NAD(+) synthetase; 6.3.5.1 (NAD(+) synthase [glutamine-hydrolyzing]; NAD(+) synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Glutamine-dependent NAD(+) synthetase; 6.3.5.1 (NAD(+) synthase [glutamine-hydrolyzing]; NAD(+) synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6IA69
ID NADE_HUMAN Reviewed; 706 AA.
AC Q6IA69; Q86SN2; Q9HA25; Q9NVM8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 3.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1;
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
DE AltName: Full=NAD(+) synthetase;
GN Name=NADSYN1;
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], SUBUNIT, MUTAGENESIS OF CYS-175,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT HIS-204.
RC TISSUE=Brain;
RX PubMed=12547821; DOI=10.1074/jbc.M209203200;
RA Hara N., Yamada K., Terashima M., Osago H., Shimoyama M., Tsuchiya M.;
RT "Molecular identification of human glutamine- and ammonia-dependent
RT NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine
RT dependency.";
RL J. Biol. Chem. 278:10914-10921(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-74 AND
RP HIS-204.
RC TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-74 AND
RP HIS-204.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-74 AND
RP HIS-204.
RC TISSUE=Lymph;
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 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 -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O =
CC AMP + diphosphate + NAD(+) + L-glutamate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.49 mM for deamido-NAD(+);
CC KM=0.089 mM for ATP;
CC KM=1.44 mM for glutamine;
CC KM=13.1 mM for ammonium;
CC Vmax=0.99 nmol/min/ug enzyme deamido-NAD(+);
CC Vmax=0.61 nmol/min/ug enzyme ATP;
CC Vmax=0.70 nmol/min/ug enzyme glutamine;
CC Vmax=1.04 nmol/min/ug enzyme ammonium;
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1.
CC -!- SUBUNIT: Homohexamer.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD
CC synthetase family.
CC -!- SIMILARITY: Contains 1 CN hydrolase domain.
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; AB091316; BAC65148.1; -; mRNA.
DR EMBL; AK001493; BAA91722.1; -; mRNA.
DR EMBL; AK022436; BAB14034.1; -; mRNA.
DR EMBL; CR457286; CAG33567.1; -; mRNA.
DR EMBL; AP000867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003638; AAH03638.1; -; mRNA.
DR EMBL; BC003666; AAH03666.1; -; mRNA.
DR RefSeq; NP_060631.2; NM_018161.4.
DR UniGene; Hs.556986; -.
DR ProteinModelPortal; Q6IA69; -.
DR SMR; Q6IA69; 5-307, 339-649.
DR IntAct; Q6IA69; 1.
DR MINT; MINT-1450170; -.
DR STRING; 9606.ENSP00000326424; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00130; L-Glutamine.
DR PhosphoSite; Q6IA69; -.
DR DMDM; 257051045; -.
DR PaxDb; Q6IA69; -.
DR PRIDE; Q6IA69; -.
DR Ensembl; ENST00000319023; ENSP00000326424; ENSG00000172890.
DR GeneID; 55191; -.
DR KEGG; hsa:55191; -.
DR UCSC; uc001oqn.3; human.
DR CTD; 55191; -.
DR GeneCards; GC11P071164; -.
DR H-InvDB; HIX0035837; -.
DR HGNC; HGNC:29832; NADSYN1.
DR HPA; CAB017798; -.
DR MIM; 608285; gene.
DR neXtProt; NX_Q6IA69; -.
DR PharmGKB; PA142671299; -.
DR eggNOG; COG0388; -.
DR HOGENOM; HOG000160137; -.
DR HOVERGEN; HBG082007; -.
DR InParanoid; Q6IA69; -.
DR KO; K01950; -.
DR OMA; DFALSCH; -.
DR OrthoDB; EOG769ZHV; -.
DR PhylomeDB; Q6IA69; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR UniPathway; UPA00253; UER00334.
DR ChiTaRS; NADSYN1; human.
DR GeneWiki; NADSYN1; -.
DR GenomeRNAi; 55191; -.
DR NextBio; 59043; -.
DR PRO; PR:Q6IA69; -.
DR ArrayExpress; Q6IA69; -.
DR Bgee; Q6IA69; -.
DR CleanEx; HS_NADSYN1; -.
DR Genevestigator; Q6IA69; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; TAS:Reactome.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
DR GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR014445; Gln-dep_NAD_synthase.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PIRSF; PIRSF006630; NADS_GAT; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding;
KW Polymorphism; Reference proteome.
FT CHAIN 1 706 Glutamine-dependent NAD(+) synthetase.
FT /FTId=PRO_0000237577.
FT DOMAIN 5 299 CN hydrolase.
FT NP_BIND 355 362 ATP (By similarity).
FT REGION 325 706 Ligase (By similarity).
FT ACT_SITE 357 357 By similarity.
FT VARIANT 74 74 V -> L (in dbSNP:rs2276360).
FT /FTId=VAR_026497.
FT VARIANT 204 204 Q -> H (in dbSNP:rs7950441).
FT /FTId=VAR_058703.
FT VARIANT 297 297 P -> L (in dbSNP:rs7121106).
FT /FTId=VAR_056204.
FT VARIANT 591 591 M -> I (in dbSNP:rs35007971).
FT /FTId=VAR_056205.
FT VARIANT 704 704 G -> S (in dbSNP:rs12282060).
FT /FTId=VAR_056206.
FT MUTAGEN 175 175 C->S: Eliminates glutamine-dependent NAD
FT synthetase activity with the ammonia-
FT dependent activity intact.
FT CONFLICT 102 102 I -> V (in Ref. 1; BAC65148).
FT CONFLICT 207 207 R -> H (in Ref. 3; CAG33567).
FT CONFLICT 623 623 W -> R (in Ref. 1; BAC65148).
SQ SEQUENCE 706 AA; 79285 MW; 9788B060F3A1D13B CRC64;
MGRKVTVATC ALNQWALDFE GNLQRILKSI EIAKNRGARY RLGPELEICG YGCWDHYYES
DTLLHSFQVL AALVESPVTQ DIICDVGMPV MHRNVRYNCR VIFLNRKILL IRPKMALANE
GNYRELRWFT PWSRSRHTEE YFLPRMIQDL TKQETVPFGD AVLVTWDTCI GSEICEELWT
PHSPHIDMGL DGVEIITNAS GSHQVLRKAN TRVDLVTMVT SKNGGIYLLA NQKGCDGDRL
YYDGCAMIAM NGSVFAQGSQ FSLDDVEVLT ATLDLEDVRS YRAEISSRNL AASRASPYPR
VKVDFALSCH EDLLAPISEP IEWKYHSPEE EISLGPACWL WDFLRRSQQA GFLLPLSGGV
DSAATACLIY SMCCQVCEAV RSGNEEVLAD VRTIVNQISY TPQDPRDLCG RILTTCYMAS
KNSSQETCTR ARELAQQIGS HHISLNIDPA VKAVMGIFSL VTGKSPLFAA HGGSSRENLA
LQNVQARIRM VLAYLFAQLS LWSRGVHGGL LVLGSANVDE SLLGYLTKYD CSSADINPIG
GISKTDLRAF VQFCIQRFQL PALQSILLAP ATAELEPLAD GQVSQTDEED MGMTYAELSV
YGKLRKVAKM GPYSMFCKLL GMWRHICTPR QVADKVKRFF SKYSMNRHKM TTLTPAYHAE
NYSPEDNRFD LRPFLYNTSW PWQFRCIENQ VLQLERAEPQ SLDGVD
//
ID NADE_HUMAN Reviewed; 706 AA.
AC Q6IA69; Q86SN2; Q9HA25; Q9NVM8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 3.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1;
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
DE AltName: Full=NAD(+) synthetase;
GN Name=NADSYN1;
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], SUBUNIT, MUTAGENESIS OF CYS-175,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT HIS-204.
RC TISSUE=Brain;
RX PubMed=12547821; DOI=10.1074/jbc.M209203200;
RA Hara N., Yamada K., Terashima M., Osago H., Shimoyama M., Tsuchiya M.;
RT "Molecular identification of human glutamine- and ammonia-dependent
RT NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine
RT dependency.";
RL J. Biol. Chem. 278:10914-10921(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-74 AND
RP HIS-204.
RC TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-74 AND
RP HIS-204.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-74 AND
RP HIS-204.
RC TISSUE=Lymph;
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 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 -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O =
CC AMP + diphosphate + NAD(+) + L-glutamate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.49 mM for deamido-NAD(+);
CC KM=0.089 mM for ATP;
CC KM=1.44 mM for glutamine;
CC KM=13.1 mM for ammonium;
CC Vmax=0.99 nmol/min/ug enzyme deamido-NAD(+);
CC Vmax=0.61 nmol/min/ug enzyme ATP;
CC Vmax=0.70 nmol/min/ug enzyme glutamine;
CC Vmax=1.04 nmol/min/ug enzyme ammonium;
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1.
CC -!- SUBUNIT: Homohexamer.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD
CC synthetase family.
CC -!- SIMILARITY: Contains 1 CN hydrolase domain.
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; AB091316; BAC65148.1; -; mRNA.
DR EMBL; AK001493; BAA91722.1; -; mRNA.
DR EMBL; AK022436; BAB14034.1; -; mRNA.
DR EMBL; CR457286; CAG33567.1; -; mRNA.
DR EMBL; AP000867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003638; AAH03638.1; -; mRNA.
DR EMBL; BC003666; AAH03666.1; -; mRNA.
DR RefSeq; NP_060631.2; NM_018161.4.
DR UniGene; Hs.556986; -.
DR ProteinModelPortal; Q6IA69; -.
DR SMR; Q6IA69; 5-307, 339-649.
DR IntAct; Q6IA69; 1.
DR MINT; MINT-1450170; -.
DR STRING; 9606.ENSP00000326424; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00130; L-Glutamine.
DR PhosphoSite; Q6IA69; -.
DR DMDM; 257051045; -.
DR PaxDb; Q6IA69; -.
DR PRIDE; Q6IA69; -.
DR Ensembl; ENST00000319023; ENSP00000326424; ENSG00000172890.
DR GeneID; 55191; -.
DR KEGG; hsa:55191; -.
DR UCSC; uc001oqn.3; human.
DR CTD; 55191; -.
DR GeneCards; GC11P071164; -.
DR H-InvDB; HIX0035837; -.
DR HGNC; HGNC:29832; NADSYN1.
DR HPA; CAB017798; -.
DR MIM; 608285; gene.
DR neXtProt; NX_Q6IA69; -.
DR PharmGKB; PA142671299; -.
DR eggNOG; COG0388; -.
DR HOGENOM; HOG000160137; -.
DR HOVERGEN; HBG082007; -.
DR InParanoid; Q6IA69; -.
DR KO; K01950; -.
DR OMA; DFALSCH; -.
DR OrthoDB; EOG769ZHV; -.
DR PhylomeDB; Q6IA69; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR UniPathway; UPA00253; UER00334.
DR ChiTaRS; NADSYN1; human.
DR GeneWiki; NADSYN1; -.
DR GenomeRNAi; 55191; -.
DR NextBio; 59043; -.
DR PRO; PR:Q6IA69; -.
DR ArrayExpress; Q6IA69; -.
DR Bgee; Q6IA69; -.
DR CleanEx; HS_NADSYN1; -.
DR Genevestigator; Q6IA69; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; TAS:Reactome.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
DR GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR014445; Gln-dep_NAD_synthase.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PIRSF; PIRSF006630; NADS_GAT; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding;
KW Polymorphism; Reference proteome.
FT CHAIN 1 706 Glutamine-dependent NAD(+) synthetase.
FT /FTId=PRO_0000237577.
FT DOMAIN 5 299 CN hydrolase.
FT NP_BIND 355 362 ATP (By similarity).
FT REGION 325 706 Ligase (By similarity).
FT ACT_SITE 357 357 By similarity.
FT VARIANT 74 74 V -> L (in dbSNP:rs2276360).
FT /FTId=VAR_026497.
FT VARIANT 204 204 Q -> H (in dbSNP:rs7950441).
FT /FTId=VAR_058703.
FT VARIANT 297 297 P -> L (in dbSNP:rs7121106).
FT /FTId=VAR_056204.
FT VARIANT 591 591 M -> I (in dbSNP:rs35007971).
FT /FTId=VAR_056205.
FT VARIANT 704 704 G -> S (in dbSNP:rs12282060).
FT /FTId=VAR_056206.
FT MUTAGEN 175 175 C->S: Eliminates glutamine-dependent NAD
FT synthetase activity with the ammonia-
FT dependent activity intact.
FT CONFLICT 102 102 I -> V (in Ref. 1; BAC65148).
FT CONFLICT 207 207 R -> H (in Ref. 3; CAG33567).
FT CONFLICT 623 623 W -> R (in Ref. 1; BAC65148).
SQ SEQUENCE 706 AA; 79285 MW; 9788B060F3A1D13B CRC64;
MGRKVTVATC ALNQWALDFE GNLQRILKSI EIAKNRGARY RLGPELEICG YGCWDHYYES
DTLLHSFQVL AALVESPVTQ DIICDVGMPV MHRNVRYNCR VIFLNRKILL IRPKMALANE
GNYRELRWFT PWSRSRHTEE YFLPRMIQDL TKQETVPFGD AVLVTWDTCI GSEICEELWT
PHSPHIDMGL DGVEIITNAS GSHQVLRKAN TRVDLVTMVT SKNGGIYLLA NQKGCDGDRL
YYDGCAMIAM NGSVFAQGSQ FSLDDVEVLT ATLDLEDVRS YRAEISSRNL AASRASPYPR
VKVDFALSCH EDLLAPISEP IEWKYHSPEE EISLGPACWL WDFLRRSQQA GFLLPLSGGV
DSAATACLIY SMCCQVCEAV RSGNEEVLAD VRTIVNQISY TPQDPRDLCG RILTTCYMAS
KNSSQETCTR ARELAQQIGS HHISLNIDPA VKAVMGIFSL VTGKSPLFAA HGGSSRENLA
LQNVQARIRM VLAYLFAQLS LWSRGVHGGL LVLGSANVDE SLLGYLTKYD CSSADINPIG
GISKTDLRAF VQFCIQRFQL PALQSILLAP ATAELEPLAD GQVSQTDEED MGMTYAELSV
YGKLRKVAKM GPYSMFCKLL GMWRHICTPR QVADKVKRFF SKYSMNRHKM TTLTPAYHAE
NYSPEDNRFD LRPFLYNTSW PWQFRCIENQ VLQLERAEPQ SLDGVD
//
MIM
608285
*RECORD*
*FIELD* NO
608285
*FIELD* TI
*608285 NAD SYNTHETASE 1; NADSYN1
*FIELD* TX
DESCRIPTION
Nicotinamide adenine dinucleotide (NAD) is a coenzyme in metabolic redox
read morereactions, a precursor for several cell signaling molecules, and a
substrate for protein posttranslational modifications. NAD synthetase
(EC 6.3.5.1) catalyzes the final step in the biosynthesis of NAD from
nicotinic acid adenine dinucleotide (NaAD).
CLONING
By searching EST databases for sequences similar to B. subtilis NAD
synthetase, followed by PCR of a fetal brain cDNA library and 5-prime
RACE of a myeloid leukemia cell cDNA library, Hara et al. (2003) cloned
NADSYN1. The deduced 706-amino acid protein contains an N-terminal
carbon-nitrogen hydrolase domain, a P-loop ATP-binding site, and a
C-terminal NAD synthase domain. Northern blot analysis detected a 3.1-kb
transcript in several mouse tissues, with highest expression in small
intestine, kidney, liver, and testis, and weaker expression in skeletal
muscle, spleen, lung, heart, and brain. Expression was also detected in
human glioma and promyelocytic leukemia cell lines.
GENE FUNCTION
By biochemical assay of recombinant epitope-tagged NADSYN1 expressed in
COS-7 cells, Hara et al. (2003) confirmed that NADSYN1 shows NAD
synthetase activity. NADSYN1 utilized both glutamine and ammonia as
amide donors. Omission of ATP, Mg(2+), or NaAD resulted in complete loss
of NAD synthesis. A mutant NADSYN1 in which cys175, corresponding to the
catalytic cysteine in nitrilases (see 604618), was replaced with ser did
not utilize glutamine. Migration of the active NADSYN1 species on a
nonreducing PAGE gel indicated that NADSYN1 forms a homohexamer.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NADSYN1
gene to chromosome 11 (TMAP RH71154).
*FIELD* RF
1. Hara, N.; Yamada, K.; Terashima, M.; Osago, H.; Shimoyama, M.;
Tsuchiya, M.: Molecular identification of human glutamine- and ammonia-dependent
NAD synthetases: carbon-nitrogen hydrolase domain confers glutamine
dependency. J. Biol. Chem. 278: 10914-10921, 2003. Note: Erratum:
J. Biol. Chem. 278: 41572 only, 2003.
*FIELD* CD
Patricia A. Hartz: 11/25/2003
*FIELD* ED
terry: 09/14/2012
alopez: 2/2/2009
mgross: 11/25/2003
*RECORD*
*FIELD* NO
608285
*FIELD* TI
*608285 NAD SYNTHETASE 1; NADSYN1
*FIELD* TX
DESCRIPTION
Nicotinamide adenine dinucleotide (NAD) is a coenzyme in metabolic redox
read morereactions, a precursor for several cell signaling molecules, and a
substrate for protein posttranslational modifications. NAD synthetase
(EC 6.3.5.1) catalyzes the final step in the biosynthesis of NAD from
nicotinic acid adenine dinucleotide (NaAD).
CLONING
By searching EST databases for sequences similar to B. subtilis NAD
synthetase, followed by PCR of a fetal brain cDNA library and 5-prime
RACE of a myeloid leukemia cell cDNA library, Hara et al. (2003) cloned
NADSYN1. The deduced 706-amino acid protein contains an N-terminal
carbon-nitrogen hydrolase domain, a P-loop ATP-binding site, and a
C-terminal NAD synthase domain. Northern blot analysis detected a 3.1-kb
transcript in several mouse tissues, with highest expression in small
intestine, kidney, liver, and testis, and weaker expression in skeletal
muscle, spleen, lung, heart, and brain. Expression was also detected in
human glioma and promyelocytic leukemia cell lines.
GENE FUNCTION
By biochemical assay of recombinant epitope-tagged NADSYN1 expressed in
COS-7 cells, Hara et al. (2003) confirmed that NADSYN1 shows NAD
synthetase activity. NADSYN1 utilized both glutamine and ammonia as
amide donors. Omission of ATP, Mg(2+), or NaAD resulted in complete loss
of NAD synthesis. A mutant NADSYN1 in which cys175, corresponding to the
catalytic cysteine in nitrilases (see 604618), was replaced with ser did
not utilize glutamine. Migration of the active NADSYN1 species on a
nonreducing PAGE gel indicated that NADSYN1 forms a homohexamer.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NADSYN1
gene to chromosome 11 (TMAP RH71154).
*FIELD* RF
1. Hara, N.; Yamada, K.; Terashima, M.; Osago, H.; Shimoyama, M.;
Tsuchiya, M.: Molecular identification of human glutamine- and ammonia-dependent
NAD synthetases: carbon-nitrogen hydrolase domain confers glutamine
dependency. J. Biol. Chem. 278: 10914-10921, 2003. Note: Erratum:
J. Biol. Chem. 278: 41572 only, 2003.
*FIELD* CD
Patricia A. Hartz: 11/25/2003
*FIELD* ED
terry: 09/14/2012
alopez: 2/2/2009
mgross: 11/25/2003