GUAA1_BACTN
ID GUAA1_BACTN Reviewed; 507 AA.
AC Q89ZV6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] 1;
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase 1;
DE AltName: Full=Glutamine amidotransferase 1;
GN Name=guaA1; OrderedLocusNames=BT_4265;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE015928; AAO79370.1; -; Genomic_DNA.
DR RefSeq; NP_813176.1; NC_004663.1.
DR RefSeq; WP_008764459.1; NC_004663.1.
DR AlphaFoldDB; Q89ZV6; -.
DR SMR; Q89ZV6; -.
DR STRING; 226186.BT_4265; -.
DR MEROPS; C26.957; -.
DR PaxDb; Q89ZV6; -.
DR PRIDE; Q89ZV6; -.
DR EnsemblBacteria; AAO79370; AAO79370; BT_4265.
DR GeneID; 60925442; -.
DR KEGG; bth:BT_4265; -.
DR PATRIC; fig|226186.12.peg.4338; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_10; -.
DR InParanoid; Q89ZV6; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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..507
FT /note="GMP synthase [glutamine-hydrolyzing] 1"
FT /id="PRO_0000140094"
FT DOMAIN 4..193
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 194..382
FT /note="GMPS ATP-PPase"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 167
FT /evidence="ECO:0000250"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT BINDING 221..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 56656 MW; 8207C222AAA741F6 CRC64;
MQEKIIILDF GSQTTQLIGR RVRELDTYCE IVPYNKFPKE DPTIKGVILS GSPFSVYDKD
AFKVDLSEIR GKYPILGICY GAQFMAYTNN GKVEPAGTRE YGRAHLTSFC KDNVLFKGVR
ENTQVWMSHG DTITAIPDNF KKIASTDKVD IAAYQVEGEK VWGVQFHPEV FHSEDGTQIL
RNFVVDVCGC KQDWSPASFI ESTVAELKAQ LGDDKVVLGL SGGVDSSVAA VLLNRAIGKN
LTCIFVDHGM LRKNEFKNVM NDYECLGLNV IGVDASEKFF AELAGVTEPE RKRKIIGKGF
IDVFDVEAHK IKDVKWLAQG TIYPDCIESL SITGTVIKSH HNVGGLPEKM HLKLCEPLRL
LFKDEVRRVG RELGMPEHLI TRHPFPGPGL AVRILGDITR EKVRILQDAD DIYIQGLRDW
GLYDQVWQAG VILLPVQSVG VMGDERTYER AVALRAVTST DAMTADWAHL PYEFLGKISN
DIINKVKGVN RVTYDISSKP PATIEWE
