GUAA_BURA4
ID GUAA_BURA4 Reviewed; 539 AA.
AC B1YS44;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=BamMC406_1891;
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001025; ACB64373.1; -; Genomic_DNA.
DR RefSeq; WP_012364116.1; NC_010551.1.
DR AlphaFoldDB; B1YS44; -.
DR SMR; B1YS44; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; ACB64373; ACB64373; BamMC406_1891.
DR KEGG; bac:BamMC406_1891; -.
DR HOGENOM; CLU_014340_0_5_4; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001680; Chromosome 1.
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..539
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000120229"
FT DOMAIN 4..202
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 203..395
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 176
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 178
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 230..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 539 AA; 59380 MW; 203D939EBC4B640E CRC64;
MHDKILILDF GSQVTQLIAR RVREAHVYCE IHPNDVSDEF VREFAPKAVI LSGSHASTYE
DHQLRAPQAV WDLGVPVLGI CYGMQTMAVQ LGGKVEWSDH REFGYAEMRA HGHTRLLDGI
EDFTTAEGHG MLKVWMSHGD KVAELPPGFA LMASTPSCPI AGMADEARGY YAVQFHPEVT
HTVKGRQIIE RFVLQIAGAK PDWIMSNHIE EAVAKIREQV GDEEVILGLS GGVDSSVAAA
LIHRAIGDQL TCVFVDHGLL RLNEGKMVLD MFEGRLHAKV VHVDASEQFL GHLTGVTDPE
AKRKIIGREF VEVFQAEAKK LSKAKWLAQG TIYPDVVESG GTKTKKATTI KSHHNVGGLP
ETLGLKLLEP LRDLFKDEVR ELGVALGLPP EMVYRHPFPG PGLGVRILGE VKREYADLLR
RADAIFIEEL RGTTATTQDA AAGLCGEADV GKTWYDLTSQ AFAVFLPVKS VGVMGDGRTY
DYVTSLRAVQ TTDFMTAHWA HLPYALLGRA SNRIINEVRG INRVVYDISG KPPATIEWE
