GUAAB_THEAC
ID GUAAB_THEAC Reviewed; 310 AA.
AC Q9HIH8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, 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=Ta1361;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(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}.
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; AL445067; CAC12482.1; -; Genomic_DNA.
DR RefSeq; WP_010901768.1; NC_002578.1.
DR AlphaFoldDB; Q9HIH8; -.
DR SMR; Q9HIH8; -.
DR STRING; 273075.Ta1361; -.
DR EnsemblBacteria; CAC12482; CAC12482; CAC12482.
DR GeneID; 1456831; -.
DR KEGG; tac:Ta1361; -.
DR eggNOG; arCOG00085; Archaea.
DR HOGENOM; CLU_014340_0_0_2; -.
DR OMA; EGGIKSH; -.
DR OrthoDB; 31932at2157; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001024; 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; Reference proteome.
FT CHAIN 1..310
FT /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT /id="PRO_0000140253"
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; 35054 MW; 2F066D2B307D3BFF CRC64;
MSTSSYIDQI KNEISEKVKG RAIIAVSGGQ DSSLLSVLAS QVLGDRLLCV FVDTGLIRIG
EVDRVRKFFE EHAMNYRIVD ASKRFLEALK GITDPEEKRK IIGKMFIDVL NEEAENFHAE
YLLQGTIAPD WIESGGQKRD TIKSHHNVGG LPKEMKLKLV EPLRDFYKDE IRAMSRELGL
RTDLQPFPGP GLAVRIVGEI TPEKLDLLRR ATRIVEDKIE SALKPEERPW QYFAVLLPVK
TTGVHGDRRA YGYTVAVRMI DSIDAMTGTF TKPSWDLLED IANTITDEIP DINRVVYDIT
NKPPATIEWE
