ID   GUAAB_PYRAB             Reviewed;         308 AA.
AC   Q9V0I7; G8ZH07;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
GN   Name=guaAB; Synonyms=guaA-C; OrderedLocusNames=PYRAB08020;
GN   ORFNames=PAB2417;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248285; CAB49716.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70202.1; -; Genomic_DNA.
DR   PIR; C75125; C75125.
DR   RefSeq; WP_010867924.1; NC_000868.1.
DR   AlphaFoldDB; Q9V0I7; -.
DR   SMR; Q9V0I7; -.
DR   STRING; 272844.PAB2417; -.
DR   EnsemblBacteria; CAB49716; CAB49716; PAB2417.
DR   GeneID; 1496146; -.
DR   KEGG; pab:PAB2417; -.
DR   PATRIC; fig|272844.11.peg.845; -.
DR   eggNOG; arCOG00085; Archaea.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   OMA; EGGIKSH; -.
DR   OrthoDB; 31932at2157; -.
DR   PhylomeDB; Q9V0I7; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
FT   CHAIN           1..308
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_0000140247"
FT   DOMAIN          1..185
FT                   /note="GMPS ATP-PPase"
FT   BINDING         28..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  34632 MW;  D5A3A59B9B3BC3B6 CRC64;
     MNWEKFVEEK VKEIRETVGD SKAIIALSGG VDSSTAAVLA YKAIGDKLHA VFVNTGFLRK
     GEPEFVVKTF RDEFGMNLHY VDAQDRFFSA LKGVTDPEEK RKIIGRVFIE VFEEVAREIG
     AEYLIQGTIA PDWIESQGKI KSHHNVGGLP ERLNLKLIEP LRDLYKDEVR ELAKFLGLPE
     KIYNRMPFPG PGLAVRVIGE VTPEKIRIVR EANAIVEEEV ERAGLRPWQA FAVLLGVKTV
     GVQGDIRAYK ETIAVRIVES LDGMTANAMN VPWEVLQRIA FRITSEIPEV GRVLYDITNK
     PPATIEFE