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Database: UniProt
Entry: F7V8K6_CLOSS
LinkDB: F7V8K6_CLOSS
Original site: F7V8K6_CLOSS 
ID   F7V8K6_CLOSS            Unreviewed;       525 AA.
AC   F7V8K6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN   OrderedLocusNames=CXIVA_04990 {ECO:0000313|EMBL:BAK46466.1};
OS   Clostridium sp. (strain SY8519).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK46466.1, ECO:0000313|Proteomes:UP000008937};
RN   [1] {ECO:0000313|Proteomes:UP000008937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX   PubMed=21914882; DOI=10.1128/JB.05637-11;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT   Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT   intestine.";
RL   J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK46466.1; -; Genomic_DNA.
DR   RefSeq; WP_013976450.1; NC_015737.1.
DR   AlphaFoldDB; F7V8K6; -.
DR   STRING; 1042156.CXIVA_04990; -.
DR   MEROPS; C26.957; -.
DR   KEGG; cls:CXIVA_04990; -.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_9; -.
DR   OMA; DQLTCMF; -.
DR   OrthoDB; 9802219at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000008937; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008937}.
FT   DOMAIN          196..389
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         223..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   525 AA;  58344 MW;  FBDF8DF332D1ACD2 CRC64;
     MARELVIVID FGGQYNQLVA RRVRENHVYC EIYSYRTDIE KIKQMNPKGI ILTGGPDSCY
     APGAASCSRE LFELGIPVLG LCYGAQLMQH ILGGEVKRAE AQEYGRTDLR VDTSAQLFAG
     VPEETTCWMS HFDYISKTAP GFEVIAATKN CPAAAVQDTE RKLYGIQFHP EVLHTPEGSR
     MLGNFVSRIC GCAGDWQIGS FVETTIQQIR EKVDSGKVLL ALSGGVDSSV AAVLMAKAVG
     SQLTCVFVDH GLLRKDEGDQ VESVFGPNGP YDLNFIRVNA QNRFYEKLAG VTEPEKKRKI
     IGEEFIRVFE EEAKKIGAVD YLVQGTIYPD VVESGLGGES AVIKSHHNVG GLPDYVDFKE
     IIEPLRDLFK DEVRRAGLEL GLPEYLVYRQ PFPGPGLGIR IIGDVTAEKV RIVQEADAIY
     REVVDHAAEN YARMHSGQEA PWKPDQYFAA LTNMRSVGVM GDERTYDYAV ALRAVRTVDF
     MTAEISRIPY DVLDKVMNRI INEVKGVNRV FYDLTSKPPG TIEFE
//
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