ID   GUAAB_METMJ             Reviewed;         305 AA.
AC   A3CWS6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B {ECO:0000255|HAMAP-Rule:MF_00345};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00345};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00345};
GN   Name=guaAB {ECO:0000255|HAMAP-Rule:MF_00345}; OrderedLocusNames=Memar_1900;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00345}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00345};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00345}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_00345}.
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DR   EMBL; CP000562; ABN57826.1; -; Genomic_DNA.
DR   RefSeq; WP_011844735.1; NC_009051.1.
DR   AlphaFoldDB; A3CWS6; -.
DR   SMR; A3CWS6; -.
DR   STRING; 368407.Memar_1900; -.
DR   EnsemblBacteria; ABN57826; ABN57826; Memar_1900.
DR   GeneID; 4848091; -.
DR   KEGG; mem:Memar_1900; -.
DR   eggNOG; arCOG00085; Archaea.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   OMA; EGGIKSH; -.
DR   OrthoDB; 31932at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002146; 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..305
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_1000048379"
FT   DOMAIN          2..184
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00345"
FT   BINDING         29..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00345"
SQ   SEQUENCE   305 AA;  33177 MW;  3C7E7255A2FD49A7 CRC64;
     MVNIEKFIDQ AVREIRDAAG EDKVVMALSG GVDSSVCAAL ATRAIGDQLV PIYVDTGLMR
     KGETDRIRSL FADANLRVVD AADEFFEALA GIVDPEEKRK AIGAKFIRIF EREAKRTGAT
     MLLQGTIYPD RIESEGGIKS HHNVGGMPLD IEFKGVIEPL ADLYKDEVRE VAGGLGLPAE
     IQHRMPFPGP GLAVRVLGEV TKEKIAIVRE ANAIVEECLV EEFRPWQCFA ALIGLGTGVK
     GDVRLHGWIV AVRAVGSRDG MTADPLLLPY ETLSRMATRI TAEIPGVARV VYDVTPKPPA
     TIEYE