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Database: UniProt
Entry: B7KSA9_METC4
LinkDB: B7KSA9_METC4
Original site: B7KSA9_METC4 
ID   B7KSA9_METC4            Unreviewed;       521 AA.
AC   B7KSA9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562, ECO:0000256|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746, ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356, ECO:0000256|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN   OrderedLocusNames=Mchl_3156 {ECO:0000313|EMBL:ACK83994.1};
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK83994.1, ECO:0000313|Proteomes:UP000002385};
RN   [1] {ECO:0000313|Proteomes:UP000002385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACK83994.1, ECO:0000313|Proteomes:UP000002385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RX   PubMed=22887658; DOI=10.1128/JB.01009-12;
RA   Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M.,
RA   Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E.,
RA   Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N.,
RA   Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M.,
RA   Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.;
RT   "Complete genome sequences of six strains of the genus Methylobacterium.";
RL   J. Bacteriol. 194:4746-4748(2012).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000256|ARBA:ARBA00002332, ECO:0000256|HAMAP-Rule:MF_00344}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC         H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00344};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153, ECO:0000256|HAMAP-
CC       Rule:MF_00344}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00344}.
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DR   EMBL; CP001298; ACK83994.1; -; Genomic_DNA.
DR   RefSeq; WP_015951353.1; NC_011757.1.
DR   AlphaFoldDB; B7KSA9; -.
DR   MEROPS; C26.957; -.
DR   KEGG; mch:Mchl_3156; -.
DR   HOGENOM; CLU_014340_0_5_5; -.
DR   OMA; DQLTCMF; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002385; Chromosome.
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; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00344; GMP_synthase; 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; IPR022955; GMP_synthase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00884; guaA_Cterm; 1.
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; PR00099; CPSGATASE.
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; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00344};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00344};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW   Rule:MF_00344};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00344};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00344};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00344}.
FT   DOMAIN          204..396
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         231..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   521 AA;  57109 MW;  F2A5C7AD70127A39 CRC64;
     MTIDTSHHDK ILIVDFGSQV TQLIARRVRE EGVYCEIVPF TKAEAAFEAH RPKGVILSGG
     PESVTTDLSP RAPQKIFESG VPVFGICYGQ QTMAAQLGGE VEGGHHAEFG RAEVEIVSDS
     PLFRGVWHAG EKYPVWMSHG DRVTKLPDGF ATIAMSRNAP FAAVADEGRH YYAVQFHPEV
     HHTPHGALLI RNFVRDIAGC SGDWTMGTYR EEAIAKIREQ VGKEKVICGL SGGVDSSVAA
     VLIHEAIGDQ LTCVFVDHGL MRLGEGDEVV RLFRDHYNIP LIHVQAQDLF IGALEGVDDP
     EVKRKTIGRL FIDVFEAEAG KIGGAAFLAQ GTLYPDVIES VSFSGGPSVT IKSHHNVGGL
     PERMNMKLVE PLRELFKDEV RLLGKELGLP ESFVGRHPFP GPGLAIRCPG MITREKLEAL
     RKADAIYLDE IRQAGLYDTI WQAFAVILPV KTVGVMGDGR TYDHVCALRA VTSVDGMTAD
     FYPFDMAFLG RVATRIINEV KGINRVTYDI TSKPPGTIEW E
//
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