GUAA_GRAFK
ID GUAA_GRAFK Reviewed; 509 AA.
AC A0M3J8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=GFO_2228;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL67193.1; -; Genomic_DNA.
DR RefSeq; WP_011710096.1; NC_008571.1.
DR AlphaFoldDB; A0M3J8; -.
DR SMR; A0M3J8; -.
DR STRING; 411154.GFO_2228; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; CAL67193; CAL67193; GFO_2228.
DR KEGG; gfo:GFO_2228; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_10; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000755; Chromosome.
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..509
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000120308"
FT DOMAIN 4..193
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 194..384
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 169
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 221..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 509 AA; 56937 MW; 996227878A18E5E3 CRC64;
MQNNVLILDF GSQYTQLIAR RVRELNIYCE IYPYHKIPED LSGFKAVILS GSPFSVRAED
APHPDLSQIR GKLPILAVCY GAQYFAHFHG GKVEPSDTRE YGRANLTVIK DAEPLFENIK
ENSQVWMSHS DSIIRLPENG VRLASTSDVL NAAYRIEGEQ TFAIQFHPEV YHSTDGKQLL
ENFLIKIAGT KATWTPGKFV DLTVSELKEK VGDDKVVLGL SGGVDSTVAA VLLHKAIGKN
LYCIFVNNGL LRKNEFESVL DQYKDMGLNV KGVDASARFL DALKGLSDPE EKRKAIGNTF
IEVFDDEAHE IKDVVYLAQG TIYPDVIESV SVNGPSVTIK SHHNVGGLPD FMKLKIVEPL
RMLFKDEVRR VGKELGIDKE LLGRHPFPGP GLAIRILGDI TEEKVRILQE VDHIFIQGLR
DWMLYDKVWQ AGAILLPIQS VGVMGDERTY EQVVALRAVE STDGMTADWV NLPYEFLQKT
SNTIINRVKG VNRVVYDISS KPPATIEWE