GUAA_VIBVY
ID GUAA_VIBVY Reviewed; 517 AA.
AC Q7MNE1;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=VV0776;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC93540.1; -; Genomic_DNA.
DR RefSeq; WP_011149610.1; NC_005139.1.
DR AlphaFoldDB; Q7MNE1; -.
DR SMR; Q7MNE1; -.
DR STRING; 672.VV93_v1c07220; -.
DR EnsemblBacteria; BAC93540; BAC93540; BAC93540.
DR KEGG; vvy:VV0776; -.
DR PATRIC; fig|196600.6.peg.791; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_6; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002675; Chromosome I.
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; Reference proteome.
FT CHAIN 1..517
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140206"
FT DOMAIN 9..199
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 200..392
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 173
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 227..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 517 AA; 57662 MW; 24C940993E8FBD17 CRC64;
MTKNIHDQRI LILDFGSQYT QLVARRVREI GVYCELWSWD VEEADIREFN PDGIILSGGP
ESVTEDNSPR APQYVFDSGV PVLGVCYGMQ TMAEQLGGKV STSDEREFGY AAVKVSGESA
IFKDLEATQD VWMSHGDKVV EIPAGFTKVG ETDTCPYAAM ANEEKKYYGV QFHPEVTHTK
NGLQMLENFV LGVCGCERLW TSESIIEDAV ARIKEQVGDD EVILGLSGGV DSSVVAMLVH
RAIGDKLTCV FVDNGLLRLN EGQQVMDMFG DKFGLNIIKV DAEERFLKAL EGKSDPEEKR
KTIGHVFVDV FDEESKKLKN AKWLAQGTIY PDVIESAASK TGKAHVIKSH HNVGGLPDDM
EMGLVEPLRE LFKDEVRKIG LELGLPYEML YRHPFPGPGL GVRVLGEIKK EYCDLLRRAD
AIFIEELHAA DLYNKVSQAF TVFLPVRSVG VMGDGRKYDW VVSLRAVETI DFMTAHWAHL
PYDFLGKVSN RIINEVNGIS RVVYDISGKP PATIEWE
