ID GUAAA_METMA Reviewed; 189 AA.
AC Q8PXF0;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 128.
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=MM_1270;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30966.1; -; Genomic_DNA.
DR RefSeq; WP_011033217.1; NC_003901.1.
DR AlphaFoldDB; Q8PXF0; -.
DR SMR; Q8PXF0; -.
DR MEROPS; C26.A31; -.
DR GeneID; 82160305; -.
DR KEGG; mma:MM_1270; -.
DR PATRIC; fig|192952.21.peg.1477; -.
DR eggNOG; arCOG00087; Archaea.
DR HOGENOM; CLU_014340_1_4_2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000595; 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 NCBIfam; TIGR00888; guaA_Nterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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..189
FT /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT /id="PRO_0000140223"
FT DOMAIN 5..189
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 168
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
SQ SEQUENCE 189 AA; 21138 MW; EC20AEAA5D487DAC CRC64;
MRELKILVVN NYGQFCHLIH RTVRDLDMDT KIIPNVTPIE EILAEEPDGL ILSGGPEMER
AGLCFDYVRE IDVPILGICL GHQAIALAYG GHVHAGKKGG YAEIEVEVLE EDDILRGLGP
KTTVWASHAD EVAILPDGFI HLARSDVCEI EAMRHPTKPI YGVQWHPEVS HTKKGEELLM
NFFEVCDLY
//
