GUAAB_METBF
ID GUAAB_METBF Reviewed; 305 AA.
AC Q46D96;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Mbar_A1178;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70146.1; -; Genomic_DNA.
DR RefSeq; WP_011306194.1; NC_007355.1.
DR AlphaFoldDB; Q46D96; -.
DR SMR; Q46D96; -.
DR STRING; 269797.Mbar_A1178; -.
DR EnsemblBacteria; AAZ70146; AAZ70146; Mbar_A1178.
DR GeneID; 3624525; -.
DR KEGG; mba:Mbar_A1178; -.
DR eggNOG; arCOG00085; Archaea.
DR HOGENOM; CLU_014340_0_0_2; -.
DR OMA; EGGIKSH; -.
DR OrthoDB; 31932at2157; -.
DR UniPathway; UPA00189; UER00296.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00958; GMP_synt_C; 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_1000048376"
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; 34093 MW; 9C4E59729124E46E CRC64;
MVKPEKFIPK AVEKISKEIK DGRAIIALSG GVDSSVCAEL AHRAIGGRLQ PIYIDTGLMR
KGETERIKHI FSHMNLDIVY AKDRFLAALK GITDPEEKRK AIGETFIRVF EEEARKLEAD
YLIQGTIYPD RIESEGGIKS HHNVGGLPSV MDFKKIVEPI EDLYKDEVRE VAWALKLPDE
ICERMPFPGP GLAVRILGEV TEEKLEVARE ANSIVEEELL DRFCPWQTFA AVIGKGTGVK
GDIRAYGWII AVRAVGSRDG MTAEALELPW DVLKKLESRI TSEIPKVARV VYDITPKPPA
TIEFE
