ID   A6UTE3_META3            Unreviewed;       310 AA.
AC   A6UTE3;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   28-JAN-2026, entry version 96.
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=Maeo_0173 {ECO:0000313|EMBL:ABR55765.1};
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanococci; Methanococcales; Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665 {ECO:0000313|EMBL:ABR55765.1, ECO:0000313|Proteomes:UP000001106};
RN   [1] {ECO:0000313|EMBL:ABR55765.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nankai-3 {ECO:0000313|EMBL:ABR55765.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000743; ABR55765.1; -; Genomic_DNA.
DR   RefSeq; WP_011972897.1; NC_009635.1.
DR   AlphaFoldDB; A6UTE3; -.
DR   STRING; 419665.Maeo_0173; -.
DR   GeneID; 5326286; -.
DR   KEGG; mae:Maeo_0173; -.
DR   eggNOG; arCOG00085; Archaea.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   OrthoDB; 33844at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001106; 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   FunFam; 3.30.300.10:FF:000002; GMP synthase [glutamine-hydrolyzing]; 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   NCBIfam; NF000848; PRK00074.1; 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   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:UP000001106}.
FT   DOMAIN          2..185
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   310 AA;  34773 MW;  8F4952C43C835DB8 CRC64;
     MMNTKEFIEE SIAEIKEQIG DKKTIIALSG GVDSAVAAVL TARAIGDQLL AVFVDTGLMR
     KNEAQEIYKI FKEDMGLNLR IIEAKEQFLK ELDGVDDPEE KRKIIGRIFI EIFEEVAKEN
     GEEVLVQGTI APDWIESEGE IKTHHNIALP SGMVLELVEP LRDLYKDEVR LLAKDLGLPD
     EIAYRQPFPG PGLAVRILGK ITEEKLEICK EANAIVEEEI EKEGLNKDLW QYFAAVLDTK
     ATGVKGDIRE YNWVVVIRFV ESLDAMTASV PELPFNIIKR ISKRITSEVP NVARVVLDVS
     DKPPATIEFE
//