GUAA_OLEA2
ID GUAA_OLEA2 Reviewed; 516 AA.
AC Q311X7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=Dde_1470;
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=21685289; DOI=10.1128/jb.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(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}.
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DR EMBL; CP000112; ABB38269.1; -; Genomic_DNA.
DR RefSeq; WP_011367436.1; NC_007519.1.
DR AlphaFoldDB; Q311X7; -.
DR SMR; Q311X7; -.
DR STRING; 207559.Dde_1470; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; ABB38269; ABB38269; Dde_1470.
DR KEGG; dde:Dde_1470; -.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_7; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002710; 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..516
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000229424"
FT DOMAIN 6..198
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 199..391
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 227..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 516 AA; 57224 MW; 6E66EB7FEDA67E4D CRC64;
MEKQNKVIIV DYGSQVTQLI ARRIREAGVY SEIHPCIVTA AEVAAMSPSA VVLSGGPASV
LGEDSPALDK GLLELGVPVL GICYGMQLLA HNLGGELSCS ETREYGPADL KFCAGSPLWD
GLKTDESSRV WMSHGDRVKK VPAGFTVTGS TETLEVAAMA DDQRRIYAVQ FHPEVHHSED
GVRMLHNFLF KIAGIKADWS MSSFCERVIK EVSEQVGPDD QVVCALSGGI DSTVVAVLLH
KAIGHRLHCI FVDNGVLRLN EVDEVSGYLR EHFDLNLTVV DARERFMKQF AGVEDPEKKR
KIIGYTFIDV FDEESQKIPN VKYLAQGTLY PDVIESISHK GPSAVIKSHH NVGGLPETMK
LKLIEPLREL FKDEVRKLAV ELGLPDFIVW RHPFPGPGLA IRVIGEVTEE RLDILRKADK
IVQNELTASG WYRKVWQGFA VLLPLKTVGV MGDDRTYEHV IALRVVDSVD AMTADWVRLP
SEVLERISSR IINEVKGVNR VVYDISSKPP STIEWE
