GUAAA_METMJ
ID GUAAA_METMJ Reviewed; 184 AA.
AC A3CTG9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000255|HAMAP-Rule:MF_01510};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_01510};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_01510};
GN Name=guaAA {ECO:0000255|HAMAP-Rule:MF_01510}; OrderedLocusNames=Memar_0736;
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_01510}.
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_01510};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01510}.
CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_01510}.
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DR EMBL; CP000562; ABN56669.1; -; Genomic_DNA.
DR RefSeq; WP_011843580.1; NC_009051.1.
DR AlphaFoldDB; A3CTG9; -.
DR SMR; A3CTG9; -.
DR STRING; 368407.Memar_0736; -.
DR EnsemblBacteria; ABN56669; ABN56669; Memar_0736.
DR GeneID; 4846221; -.
DR KEGG; mem:Memar_0736; -.
DR eggNOG; arCOG00087; Archaea.
DR HOGENOM; CLU_014340_1_4_2; -.
DR OMA; GPDMDRI; -.
DR OrthoDB; 79931at2157; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002146; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01510; GMP_synthase_A; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR023686; GMP_synthase_A.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..184
FT /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT /id="PRO_0000294267"
FT DOMAIN 3..184
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
SQ SEQUENCE 184 AA; 19764 MW; 86F8B26A50B931C0 CRC64;
MLPLYVVNNH GQFNHLILRT LRDMDIEATM ISNETPPAEV ARGCRGIVLG GGPTLERAGV
ASAYLDLGLP VLGICLGLHI MATARGGAIR RGASGGFGAV EVEIFEQNPL LRGYPDRMQV
WASHADEVSV VPEGFVRLAG SSICGVEAMA SPDEHLYGIQ WHPEVSHTVN GRLLFENFDG
ICSE