ID   GUAAB_HALSA             Reviewed;         305 AA.
AC   Q9HP33;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
GN   Name=guaAB; OrderedLocusNames=VNG_1829G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(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; AE004437; AAG20037.1; -; Genomic_DNA.
DR   PIR; A84334; A84334.
DR   RefSeq; WP_010903336.1; NC_002607.1.
DR   AlphaFoldDB; Q9HP33; -.
DR   SMR; Q9HP33; -.
DR   STRING; 64091.VNG_1829G; -.
DR   PaxDb; Q9HP33; -.
DR   EnsemblBacteria; AAG20037; AAG20037; VNG_1829G.
DR   GeneID; 5953124; -.
DR   GeneID; 62885055; -.
DR   KEGG; hal:VNG_1829G; -.
DR   PATRIC; fig|64091.14.peg.1394; -.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   InParanoid; Q9HP33; -.
DR   OMA; EGGIKSH; -.
DR   OrthoDB; 31932at2157; -.
DR   PhylomeDB; Q9HP33; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000554; Chromosome.
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:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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..305
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_0000140239"
FT   DOMAIN          2..185
FT                   /note="GMPS ATP-PPase"
FT   BINDING         29..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  33725 MW;  D47A25946A0869ED CRC64;
     MVDVDSFVED ARAEISEALG DETAIIALSG GVDSSTAAAL AYEAVGDQLV PVYVDTGLMR
     KGETDEIREV FDYMDSLRVV DASDRFFDEL AGVTDPEEKR HAIGEQFIRE FETVAEEVDA
     TQLVQGTIYP DRIESEGTIK SHHNVGGLPE RVGFEGIVEP MRDLYKDEVR EVARHLGLEE
     IISERMPFPG PGLAVRVIGE VTPEKVAVCR EATHIVEDEL EAYEPWQAFA AVLGRATGVK
     GDNRVHGHVV AVRSVESRDG MTARAQELEW ETLQRLQSRI AGTIDEVSRV VYDVTHKPPA
     TIEYE