GUAA_BACFR
ID GUAA_BACFR Reviewed; 507 AA.
AC Q64XQ7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, 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=BF0969;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD47719.1; -; Genomic_DNA.
DR RefSeq; WP_005785252.1; NZ_UYXF01000032.1.
DR RefSeq; YP_098253.1; NC_006347.1.
DR AlphaFoldDB; Q64XQ7; -.
DR SMR; Q64XQ7; -.
DR STRING; 295405.BF0969; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; BAD47719; BAD47719; BF0969.
DR GeneID; 66330052; -.
DR KEGG; bfr:BF0969; -.
DR PATRIC; fig|295405.11.peg.969; -.
DR HOGENOM; CLU_014340_0_5_10; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002197; 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..507
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000229403"
FT DOMAIN 4..193
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 194..382
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 507 AA; 56437 MW; 37A03CD2661B5A94 CRC64;
MQEKIIILDF GSQTTQLIGR RVRELDTYCE IVPYNKFPKG DETVKGVILS GSPFSVYDES
AFKVDLSEIR GKYPILGICY GAQFMAYTNG GKVEPAGTRE YGRAHLTSFC KDNVLFKGVR
EGTQVWMSHG DTITAIPENF KTIASTDKVA IAAYQVEGEQ VWGVQFHPEV FHSEDGTQML
RNFVVDVCGC KQDWSPASFI ESTVAELKAQ LGDDKVVLGL SGGVDSSVAA VLLNRAIGKN
LTCIFVDHGM LRKNEFKNVM HDYECLGLNV IGVDASEKFF SELEGVTEPE RKRKIIGKGF
IDVFDEEAHK LKDVKWLAQG TIYPDCIESL SITGTVIKSH HNVGGLPEKM NLKLCEPLRL
LFKDEVRRVG RELGMPEHLI TRHPFPGPGL AVRILGDITP EKVRILQDAD DIFIQGLRDW
GLYDQVWQAG VILLPVQSVG VMGDERTYER AVALRAVTST DAMTADWAHL PYEFLGKVSN
DIINKVKGVN RVTYDISSKP PATIEWE
