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Database: UniProt
Entry: GUAA_PSESM
LinkDB: GUAA_PSESM
Original site: GUAA_PSESM 
ID   GUAA_PSESM              Reviewed;         525 AA.
AC   Q886X5;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 130.
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=PSPTO_1450;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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; AE016853; AAO54971.1; -; Genomic_DNA.
DR   RefSeq; NP_791276.1; NC_004578.1.
DR   RefSeq; WP_005771001.1; NC_004578.1.
DR   AlphaFoldDB; Q886X5; -.
DR   SMR; Q886X5; -.
DR   STRING; 223283.PSPTO_1450; -.
DR   MEROPS; C26.957; -.
DR   GeneID; 1183087; -.
DR   KEGG; pst:PSPTO_1450; -.
DR   PATRIC; fig|223283.9.peg.1470; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_6; -.
DR   OMA; DQLTCMF; -.
DR   OrthoDB; 9802219at2; -.
DR   PhylomeDB; Q886X5; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; ISS:JCVI.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009152; P:purine ribonucleotide biosynthetic process; ISS:JCVI.
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; IPR022310; NAD/GMP_synthase.
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   Pfam; PF02540; NAD_synthase; 1.
DR   PRINTS; PR00099; CPSGATASE.
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; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..525
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140164"
FT   DOMAIN          9..207
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          208..400
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        181
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         235..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   525 AA;  58117 MW;  41E607B35D450B1A CRC64;
     MALDIHAHRI LILDFGSQYT QLIARRVREI GVYCELHPFD MDDEAIREFA PKGVILAGGP
     ESVHEANSPR CPQAVFDLGV PVFGICYGMQ TMAEQLGGKV AGSELREFGY ARVDVVGKSR
     LLDGIEDHID ADGLFGLDVW MSHGDKVTKL PEDFHILAST PSCPIAGMAD DARGYYGVQF
     HPEVTHTKQG GRILSRFILD ICGCEALWTP SKIAEDAIAQ VRAQVGTDSV LLGLSGGVDS
     SVVAALLHKA IGDQLTCVFV DNGLLRLHEG EQVMAMFAEN MGVKVIRANA EEQFLNNLEG
     ESDPEKKRKI IGRTFIDVFD AESCKLDNIK YLAQGTIYPD VIESAGAKSG KAHVIKSHHN
     VGGLPEEMNL KLVEPLRELF KDEVRRLGLE LGLPYDMVYR HPFPGPGLGV RILGEVKKEY
     ADILRRADHI FIEELRKADW YHKVSQAFVV FQPVKSVGVV GDGRRYAWVV ALRAVETIDF
     MTARWAHLPY ELLETVSGRI INEIEGISRV TYDVSSKPPA TIEWE
//
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