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
//