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Database: UniProt
Entry: I7GYZ6_9HELI
LinkDB: I7GYZ6_9HELI
Original site: I7GYZ6_9HELI 
ID   I7GYZ6_9HELI            Unreviewed;       583 AA.
AC   I7GYZ6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 74.
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   ECO:0000313|EMBL:BAM32161.1};
GN   ORFNames=HCBAA847_0923 {ECO:0000313|EMBL:BAM32161.1};
OS   Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM32161.1, ECO:0000313|Proteomes:UP000006036};
RN   [1] {ECO:0000313|EMBL:BAM32161.1, ECO:0000313|Proteomes:UP000006036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM32161.1,
RC   ECO:0000313|Proteomes:UP000006036};
RX   PubMed=23012276; DOI=10.1128/JB.01347-12;
RA   Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT   "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT   BAA-847.";
RL   J. Bacteriol. 194:5692-5692(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; AP012492; BAM32161.1; -; Genomic_DNA.
DR   RefSeq; WP_002956568.1; NZ_DS990392.1.
DR   AlphaFoldDB; I7GYZ6; -.
DR   MEROPS; C26.957; -.
DR   KEGG; hcb:HCBAA847_0923; -.
DR   PATRIC; fig|1206745.3.peg.966; -.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_7; -.
DR   OrthoDB; 9802219at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000006036; Chromosome 1.
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; 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   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; 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          264..458
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         291..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   583 AA;  64858 MW;  0C2F99B9188F978E CRC64;
     MRLDSHFVEI LVLDFGSQYT QLIARRLREY GIYTEIVPYF EKLDSIKAKN PKGIILSGGP
     ASVYEEGAYK PDSRVFELGV PVLGICYGMQ YIAHFFGGSV VRAEAQEFGK AVLEIAESSV
     DFGLFKGVKQ DSIVWMSHAD KVESLPSGFV ELAKSGNTHY CAIADFKRNV YALQFHPEVV
     HSECGGEMLK NFAVGICGAD TSWNMRNFAE SEIAKLREKV LGDSKKVDSK PTQENLQEKG
     LDSNAEGFCD DFKGCADFEA RSLLNINDEA TKSNSLKNTQ KPTQKVLCAV SGGVDSSVVA
     ILLYRAIGEN LIPVFVDTGL LRKGEREAVE AMFKENLKVP LIVADARELF LRRLKGVTEP
     EQKRKIIGET FIEVFEAEAK KHNTKGEIKF LAQGTLYPDV IESVSVKGPS KTIKSHHNVG
     GLPEWMKFEL IEPLRELFKD EVRALGRELG MPESMLMRHP FPGPGLAIRI MGEVNAADLE
     LLKEADSIFI EELHKWGLYD SVWQAFCVLL NVRSVGVMGD NRTYDNTICV RAVEAQDGMT
     ASFLHLPHAF LESVSNRIIN EVAGINRVVY DITSKPPGTI EWE
//
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