GUAAB_PYRFU
ID GUAAB_PYRFU Reviewed; 313 AA.
AC Q8U0R8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
GN Name=guaAB; OrderedLocusNames=PF1516;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(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: Heterodimer composed of a glutamine amidotransferase subunit
CC (A) and a GMP-binding subunit (B). {ECO:0000305}.
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DR EMBL; AE009950; AAL81640.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8U0R8; -.
DR SMR; Q8U0R8; -.
DR STRING; 186497.PF1516; -.
DR EnsemblBacteria; AAL81640; AAL81640; PF1516.
DR KEGG; pfu:PF1516; -.
DR PATRIC; fig|186497.12.peg.1579; -.
DR eggNOG; arCOG00085; Archaea.
DR HOGENOM; CLU_014340_0_0_2; -.
DR OMA; EGGIKSH; -.
DR PhylomeDB; Q8U0R8; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001013; 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 CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00345; GMP_synthase_B; 1.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR026598; GMP_synthase_B.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 2.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; GMP biosynthesis; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..313
FT /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT /id="PRO_0000140248"
FT DOMAIN 6..190
FT /note="GMPS ATP-PPase"
FT BINDING 33..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 35282 MW; 8BFAF701EBC3CD3F CRC64;
MKRWVKVWEK FIEEKIREIR ETVGDSKAII ALSGGVDSST AAVLAHRAIG DRLHAVFVNT
GFLRKGEPEF VIKTFRDEFG MNLHYVDAQD RFFAALKGVT DPEEKRKIIG RVFIEVFEEV
AKDIGAEYLI QGTIAPDWIE SQGKIKSHHN VGGLPEKLNL KIIEPLRDLY KDEVRQLAKE
LGLPEKIYNR MPFPGPGLAV RVIGEVTPEK IRIVREANAI VEEEIEKAGL RPWQAFAVLL
GVKTVGVQGD IRAYKETIAV RIVESVDGMT ANAMNVPWEV LQRIAFRITS EIPEVGRVLY
DITNKPPATI EFE
