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Database: UniProt
Entry: K1R7T0_CRAGI
LinkDB: K1R7T0_CRAGI
Original site: K1R7T0_CRAGI 
ID   K1R7T0_CRAGI            Unreviewed;       834 AA.
AC   K1R7T0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE            EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN   ORFNames=CGI_10025128 {ECO:0000313|EMBL:EKC39669.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC39669.1};
RN   [1] {ECO:0000313|EMBL:EKC39669.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC39669.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
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DR   EMBL; JH816450; EKC39669.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1R7T0; -.
DR   HOGENOM; CLU_014340_0_2_1; -.
DR   InParanoid; K1R7T0; -.
DR   OMA; HIVHRHP; -.
DR   UniPathway; UPA00189; UER00296.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.30.300.10; -; 2.
DR   Gene3D; 3.40.50.880; -; 2.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 2.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 2.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}.
FT   ACT_SITE        96
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         200..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   834 AA;  92375 MW;  696315A1DB322C64 CRC64;
     MNGTDNGGFI NGSGDNRERV AILDAGAQYG KVIDRRVREL FVESQILPLD TPAFTLKEEG
     YRAIIISGGP NSVYAENAPR YDPEIFVCGL PVLGICYGMQ KEQNVLLTHG DSIDTVANGF
     TAIAHSGKII AGIANEEKKL FGLQFHPEVD LTDQGKEMMS HFLFDVAKCK GTFTMQGREA
     ECLKYITEVT GNHKVLMLLS GGVDSTVCAA LLHKALTKEQ VIAVHIDNGF MRKNESQNVV
     QSLNKIGLNV KVVKAAHTFY NGSTSISVKT GDSTPRKRKT ERLNTVVCPE EKRKIIGDTF
     MRVANEVLEE LNLKPEDVYL GQGTLRPDLI ESASELASGK ADAIKTHHND TELVRELRRQ
     GRVVEPLKDF HKDEVRTIGK DLGLPPELVH RHPFPGPGLA IRVICAEEAY MCKDFAETSI
     LLKFLMDFSN SVKTPHTLIT RLKNSTSEEE QQQLKRISEE AQLFSTLLPI KTVGVQGDCR
     TYSYVVGISS DSEPNWENLM ILAKLIPRIC HNINRVVYIF GGSVRFPVED ITPTYLTNGV
     LSTLRQADYL ATEVLHATNT TSSLSQMPVI IIPVHFDRDP VKNSPSCQRS IVIRTFITND
     FMTGIAATPN KQFPAQDADA SCRACLTETC IAQSEPMTEP HRIWAARDDT VQPITDVGPK
     YSRAGLESHA YEEYDDYYGD DFYYQEYPEP EEPTLISSQK LSGTSNCKKN YKEAQASGES
     KGPLTEGSCP IASCQTPKSE SEAATLCPFL LSVNKKSLQT DGFLNAIVSE VESGFPKLEK
     ILHHHYLSSD EADVTISGKE GKHSYKLKNF SKLSSEQIGR AVGRYIFNKA KPKQ
//
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