GUAA_HELPS
ID GUAA_HELPS Reviewed; 508 AA.
AC B2UUF1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=HPSH_05360;
OS Helicobacter pylori (strain Shi470).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=512562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shi470;
RA Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT Asian ancestry of the first Americans.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR EMBL; CP001072; ACD48483.1; -; Genomic_DNA.
DR RefSeq; WP_000604638.1; NC_010698.2.
DR AlphaFoldDB; B2UUF1; -.
DR SMR; B2UUF1; -.
DR MEROPS; C26.957; -.
DR KEGG; hps:HPSH_05360; -.
DR HOGENOM; CLU_014340_0_5_7; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 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 Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..508
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000120319"
FT DOMAIN 1..189
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 190..383
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 217..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 508 AA; 56839 MW; F945DE8AA89D640E CRC64;
MILVLDFGSQ YTQLIARRLR ESGIYAEIVP FFESIENIQK KAPKGLILSG GPASVYAKDA
YKPSKKIFDL DLPILGICYG MQYLVDFFGG VVACTNEQEF GKAILEITQD SVIFEGVKIK
SLVWMSHMDK VIELPKGFTT LAKSPNSPHC AIENAKIFGL QFHPEVIQSE EGGKILENFA
LLVCGCEKTW GMQHFAQKEM ARLKEKIANA KVLCAVSGGV DSTVVATLLH RAIKDNLIAV
FVDHGLLRKN EKEKVQAMFK DLQIPLNTID AKEIFLSKLK GVSEPELKRK IIGETFIEAF
EKEAKKHHLK GKIEFLAQGT LYPDVIESVS VKGPSKVIKT HHNVGGLPEW MDFKLIEPLR
ELFKDEVRLL GKELGISQDF LMRHPFPGPG LAIRILGEVS ESKIRCLQEA DFIFIEELKK
ANLYDKVWQA FCVLLNVNSV GVMGDNRTYE NAICLRAVNA SDGMTASFSF LEHSFLEKVS
NRITNEVSGI NRVVYDITSK PPGTIEWE
