GUAA_AFIC5
ID GUAA_AFIC5 Reviewed; 531 AA.
AC B6JHM4; F8BZA3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=OCAR_6467, OCA5_c15850;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=18539730; DOI=10.1128/jb.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001196; ACI93580.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI06299.1; -; Genomic_DNA.
DR RefSeq; WP_012563606.1; NC_015684.1.
DR AlphaFoldDB; B6JHM4; -.
DR SMR; B6JHM4; -.
DR STRING; 504832.OCAR_6467; -.
DR MEROPS; C26.A07; -.
DR EnsemblBacteria; AEI06299; AEI06299; OCA5_c15850.
DR KEGG; oca:OCAR_6467; -.
DR KEGG; ocg:OCA5_c15850; -.
DR PATRIC; fig|504832.7.peg.1688; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_5; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000007730; 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..531
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000120348"
FT DOMAIN 20..213
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 214..406
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 187
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 189
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 241..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 531 AA; 57834 MW; BA80A10B1DD8619A CRC64;
MTAPRQSTSA TPDVAAAHDK ILIVDFGSQV TQLIARRVRE EGVYSEIVPF QKAEQAFTAM
QPKAVILSGG PASVLEAGAP SAPMSIFTAG VPVLGICYGE QTMAQQLGGM VEGGHHREFG
RAAIEITDDC ALFEGVWKKG EQHDVWMSHG DRVTKLPEGF RGVARAAGSP IAIIADDTRK
FYAMQFHPEV VHTPDGAKLI RNFVRKVAGL KGDWTMRAFR EEAIEKIRAQ VGQGRVICGL
SGGVDSAVAA VLIHEAIGDQ LTCVFVDHGL LRMAEAETVV SLFRDHYNIP LVHVDASKTF
LGELAGVTDP ELKRKTIGRL FIDVFDEEAK KIGGADFLAQ GTLYPDVIES VSFTGGPSVT
IKSHHNVGGL PARMKMKLVE PLRELFKDEV RALGRELGLP DVFVGRHPFP GPGLAIRCPG
EITPEKLDIL RQADAIYIEE IRRAGLYDTI WQAFAVLLPV KTVGVMGDGR TYEFVVGLRA
VTSTDGMTAD FYPFDMRFLG ETATRIINEV KGVNRVVYDV TSKPPGTIEW E
