GUAAB_THEVO
ID GUAAB_THEVO Reviewed; 310 AA.
AC Q97C09;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
GN Name=guaAB; OrderedLocusNames=TV0296; ORFNames=TVG0306280;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB59438.1; -; Genomic_DNA.
DR RefSeq; WP_010916551.1; NC_002689.2.
DR AlphaFoldDB; Q97C09; -.
DR SMR; Q97C09; -.
DR STRING; 273116.14324511; -.
DR EnsemblBacteria; BAB59438; BAB59438; BAB59438.
DR GeneID; 1440809; -.
DR KEGG; tvo:TVG0306280; -.
DR eggNOG; arCOG00085; Archaea.
DR HOGENOM; CLU_014340_0_0_2; -.
DR OMA; EGGIKSH; -.
DR OrthoDB; 31932at2157; -.
DR PhylomeDB; Q97C09; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001017; 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; 1.
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.
FT CHAIN 1..310
FT /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT /id="PRO_0000140254"
FT DOMAIN 1..187
FT /note="GMPS ATP-PPase"
FT BINDING 27..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 34643 MW; A451A9E750C73C09 CRC64;
MSFSDYISRI KDNIRNSIKG KAIIAVSGGQ DSSLLSLLAS EVLGNNLLCV FIDTGLLRKN
ETGRVKDFFE KHSMNYVIVD AADTFINNLK GVTDPEEKRK IIGKTFIDVL SEQAQNFGAE
YLLQGTIAPD WIESGGQKRD TIKSHHNVGG LPKDMKLKLV EPLRDYYKDE IRGMSKELGL
PTDIQPFPGP GLAVRIIGEV TKEKLDLLRA VTDIVERKIS EAMPSESRPW QYFAVLLPVR
TTGVHGDRRA YGLTVGIRMI ETTDAMTGTF SKPSWDLLED ISNTITDEIP EINRVVYDIT
NKPPATIEWE
