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Database: UniProt
Entry: B2RRH9_MOUSE
LinkDB: B2RRH9_MOUSE
Original site: B2RRH9_MOUSE 
ID   B2RRH9_MOUSE            Unreviewed;       693 AA.
AC   B2RRH9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 123.
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   Name=Gmps {ECO:0000313|EMBL:AAI38412.1, ECO:0000313|MGI:MGI:2448526};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI38412.1};
RN   [1] {ECO:0000313|EMBL:AAI38412.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI38412.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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; BC138411; AAI38412.1; -; mRNA.
DR   EMBL; BC138412; AAI38413.1; -; mRNA.
DR   RefSeq; NP_001028472.2; NM_001033300.2.
DR   AlphaFoldDB; B2RRH9; -.
DR   SMR; B2RRH9; -.
DR   MEROPS; C26.950; -.
DR   SwissPalm; B2RRH9; -.
DR   PeptideAtlas; B2RRH9; -.
DR   Antibodypedia; 33632; 285 antibodies from 33 providers.
DR   GeneID; 229363; -.
DR   KEGG; mmu:229363; -.
DR   AGR; MGI:2448526; -.
DR   CTD; 8833; -.
DR   MGI; MGI:2448526; Gmps.
DR   VEuPathDB; HostDB:ENSMUSG00000027823; -.
DR   HOGENOM; CLU_014340_0_2_1; -.
DR   OMA; DQLTCMF; -.
DR   OrthoDB; 6206at2759; -.
DR   UniPathway; UPA00189; UER00296.
DR   BioGRID-ORCS; 229363; 23 hits in 80 CRISPR screens.
DR   ChiTaRS; Gmps; mouse.
DR   ExpressionAtlas; B2RRH9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:Ensembl.
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; -; 1.
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   NCBIfam; TIGR00888; guaA_Nterm; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
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   1: Evidence at protein level;
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   DOMAIN          217..435
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         244..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   693 AA;  76723 MW;  854DBAD6A9C75A12 CRC64;
     MALCNGDSKP ENAGGDLKDG SHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
     AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPI LGICYGMQMM NKVFGGTVHK
     KSVREDGVFN ISMDNTCSLF RGLQKEEIVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE
     SKKLYGVQFH PEVGLTENGK VILKNFLYDI AGCSGNFTVQ NRELECIREI KEKVGTSKVL
     VLLSGGVDST VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
     HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMSLKPE
     EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR
     ILGRELDLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH
     TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW
     ESLIFLARLI PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
     ESGFAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGVP ATPGNEIPVE
     VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
//
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