GUAA_DEIRA
ID GUAA_DEIRA Reviewed; 506 AA.
AC Q9RT91;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=guaA; OrderedLocusNames=DR_1874;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE000513; AAF11428.1; -; Genomic_DNA.
DR PIR; B75342; B75342.
DR RefSeq; NP_295597.1; NC_001263.1.
DR RefSeq; WP_010888509.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RT91; -.
DR SMR; Q9RT91; -.
DR STRING; 243230.DR_1874; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; AAF11428; AAF11428; DR_1874.
DR KEGG; dra:DR_1874; -.
DR PATRIC; fig|243230.17.peg.2086; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_0; -.
DR InParanoid; Q9RT91; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002524; Chromosome I.
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..506
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140121"
FT DOMAIN 2..190
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 191..381
FT /note="GMPS ATP-PPase"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /evidence="ECO:0000250"
FT ACT_SITE 167
FT /evidence="ECO:0000250"
FT BINDING 219..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 506 AA; 55513 MW; F54B689D18889F4C CRC64;
MSIVILDFGS QFTRLITRRF RELGAYSVIL PGTASLERIQ QENPQGIVLS GGPSSVYDEG
APRPAPGVLD LNVPILGVCY GMQYLAHEAG GDVKRAGKRE YGKADLTEYG GRLFEGIQGE
FVAWMSHSDS VTQLPQGYQV VARTEHTPVT AIENNDTRRY GVQFHPEVVH TPKGGQMLAN
FLDICGVTRD WNAEHIVDEL IEGVRAQVGD TGRVLLGISG GVDSSTLALL LAKAVGERLT
AVFIDHGLLR LGEREQVEAA LTPLGVNLVT VDAKDEFLGQ LAGVSDPEQK RKIIGREFIR
AFERETAKLG DFEFLAQGTL YPDVIESAGG EGAANIKSHH NVGGLPDDVQ FKLVEPFRTL
FKDEVREIAR LLGLPDHIRM RHPFPGPGLA IRCLGEVTAE KVDILQRVDD IFISGLREFG
LYDGCSQALA VLTPIQSVGV MGDERTYSYT AALRAVTTDD FMTAEWARLP YDFLATMSNR
IVNQVHEINR VVYDITGKPP ATIEWE
