ID   Q2FSE7_METHJ            Unreviewed;       305 AA.
AC   Q2FSE7;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   18-JUN-2025, entry version 108.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B {ECO:0000256|ARBA:ARBA00022411, ECO:0000256|HAMAP-Rule:MF_00345};
DE            EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746, ECO:0000256|HAMAP-Rule:MF_00345};
DE   AltName: Full=GMP synthetase {ECO:0000256|ARBA:ARBA00030464, ECO:0000256|HAMAP-Rule:MF_00345};
GN   Name=guaAB {ECO:0000256|HAMAP-Rule:MF_00345};
GN   OrderedLocusNames=Mhun_2527 {ECO:0000313|EMBL:ABD42227.1};
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD42227.1, ECO:0000313|Proteomes:UP000001941};
RN   [1] {ECO:0000313|Proteomes:UP000001941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC   {ECO:0000313|Proteomes:UP000001941};
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000256|ARBA:ARBA00002332, ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00049404, ECO:0000256|HAMAP-
CC         Rule:MF_00345};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153, ECO:0000256|HAMAP-
CC       Rule:MF_00345}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000256|ARBA:ARBA00011264,
CC       ECO:0000256|HAMAP-Rule:MF_00345}.
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DR   EMBL; CP000254; ABD42227.1; -; Genomic_DNA.
DR   RefSeq; WP_011449485.1; NC_007796.1.
DR   AlphaFoldDB; Q2FSE7; -.
DR   FunCoup; Q2FSE7; 195.
DR   STRING; 323259.Mhun_2527; -.
DR   EnsemblBacteria; ABD42227; ABD42227; Mhun_2527.
DR   GeneID; 3922313; -.
DR   KEGG; mhu:Mhun_2527; -.
DR   eggNOG; arCOG00085; Archaea.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   InParanoid; Q2FSE7; -.
DR   OrthoDB; 33844at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001941; 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; 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   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00345};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW   Rule:MF_00345};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00345};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00345};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00345}; Reference proteome {ECO:0000313|Proteomes:UP000001941}.
FT   DOMAIN          2..184
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   BINDING         29..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   305 AA;  33567 MW;  7E89970B9AC70744 CRC64;
     MVNTEKFIKE AIHRIQEESN GEKVVIALSG GVDSSVCAEL ASRAIGERLI PIYVDTGLMR
     KGETKRISEI FGHLGLKVVN AADEFLDALE GESDPEKKRK IVGERFIRVF EREATATGAQ
     YLLQGTIYPD CIESEGGIKS HHNVGGLPLT MQFQGVIEPL RDLYKDEVRE VAEALGLPRE
     IAHRMPFPGP GLSVRVVGKV TREAIDVVRE ANAIIEEVLV EKYRPWQCLG ALVGLGTGVK
     GDNRLHGWIV AVRAVNSRDG MTADPIEISF QDLQEIESRI TSSIPSVARV VYDVTPKPPA
     TIEYE
//