GUAA_BRASO
ID GUAA_BRASO Reviewed; 535 AA.
AC A4YSU1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=BRADO3169;
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=114615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CU234118; CAL76967.1; -; Genomic_DNA.
DR RefSeq; WP_011926132.1; NC_009445.1.
DR AlphaFoldDB; A4YSU1; -.
DR SMR; A4YSU1; -.
DR STRING; 114615.BRADO3169; -.
DR EnsemblBacteria; CAL76967; CAL76967; BRADO3169.
DR KEGG; bra:BRADO3169; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_5; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR BioCyc; BSP114615:BRADO_RS14850-MON; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001994; 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; Reference proteome.
FT CHAIN 1..535
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000120224"
FT DOMAIN 24..217
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 218..410
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 191
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 193
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 245..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 535 AA; 58291 MW; 58FF71833CE26A9E CRC64;
MTAPANNTPA AAATDTSVAA LHDKILIVDF GSQVTQLIAR RVREDGVYCE IVPFQKAEAA
FRQMNPKAVI LSGGPESVHE EGSPRAPQLI FESGVPVMGI CYGQMTMAAQ LGGTVEGGHH
REFGRADVEV KTNSLLFDGV WQPGEQHQVW MSHGDRITQM PPGFSVAGVS PNAPFAVIQD
EARKYYGLMF HPEVVHTPDG AKLIRNFVRN ISGLGGDWTM HAFREEEIKK IRAQVGQGKV
ICGLSGGVDS AVAAVLIHEA IGDQLTCVFV DHGLLRLNEA ETVVDLFRHH YNIPLVHVDA
SKLFLGELAG VTDPEAKRKT IGRLFIDVFE AEAKKIGGAD FLAQGTLYPD VIESVSFTGG
PSVTIKSHHN VGGLPARMNM KLVEPLRELF KDEVRVLGRE LGLPDVFVGR HPFPGPGLAI
RCPGEITTDK LDILRKADAI YIDEIRKAGL YDTIWQAFAV LLPVKTVGVM GDGRTYDYVV
GLRAVTSTDG MTADFYPFDM KFLGNTATRI INEVKGVNRV VYDVTSKPPG TIEWE
