ID   GUAAB_METPE             Reviewed;         305 AA.
AC   B8GIB2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   10-JUN-2026, entry version 81.
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};
GN   OrderedLocusNames=Mpal_0069;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00345}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP +
CC         diphosphate + 2 H(+); 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}.
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; CP001338; ACL15463.1; -; Genomic_DNA.
DR   RefSeq; WP_012616782.1; NC_011832.1.
DR   AlphaFoldDB; B8GIB2; -.
DR   SMR; B8GIB2; -.
DR   STRING; 521011.Mpal_0069; -.
DR   GeneID; 7272238; -.
DR   KEGG; mpl:Mpal_0069; -.
DR   eggNOG; arCOG00085; Archaea.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   OrthoDB; 33844at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002457; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.30.300.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00345; GMP_synthase_B; 1.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR026598; GMP_synthase_B.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 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_1000133394"
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;  33478 MW;  4DA8222FD003A153 CRC64;
     MVNTERFIQQ AVSEIRELTA DARVVMALSG GVDSSVCAAL AAQAIGERLE PIYVDTGLMR
     KGETDRIRHL FGHLNLRIVD ASDEFLDALA GVADPETKRK IIGERFIRVF EREAEKTGAT
     VLLQGTIYPD RIESEGGIKS HHNVGGMPLG IAFTQVLEPL RDLYKDEVRE VAGALGLPRE
     IQHRMPFPGP GLAVRIIGEV TREKVAVIRE ANAITEEELV EEFRPWQCLA ALVGLGTGVK
     GDIRLHGWIV AVRAVNSRDG MTADPLEVPY PVLFKIASRI TAEIPSVARV VYDVTPKPPA
     TIEYE
//