GUAAA_METHJ
ID GUAAA_METHJ Reviewed; 188 AA.
AC Q2FL30;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Mhun_1588;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
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. {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; CP000254; ABD41319.1; -; Genomic_DNA.
DR RefSeq; WP_011448584.1; NC_007796.1.
DR AlphaFoldDB; Q2FL30; -.
DR SMR; Q2FL30; -.
DR STRING; 323259.Mhun_1588; -.
DR MEROPS; C26.A31; -.
DR EnsemblBacteria; ABD41319; ABD41319; Mhun_1588.
DR GeneID; 3923844; -.
DR KEGG; mhu:Mhun_1588; -.
DR eggNOG; arCOG00087; Archaea.
DR HOGENOM; CLU_014340_1_4_2; -.
DR OMA; GPDMDRI; -.
DR OrthoDB; 79931at2157; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001941; 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; Reference proteome.
FT CHAIN 1..188
FT /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT /id="PRO_0000294268"
FT DOMAIN 3..188
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 188 AA; 20428 MW; EDA84824871ADEF0 CRC64;
MLPLYVVNNY GQFNHLILRA LRDLDIDAKL IPNTTPVSEV REGCQGIILG GGPDISRAGL
SHEYVRLGKP VLGICLGLHV IAQEFGGTVQ SGQKGGYGAV EVTITDHDGI LQGYPQTMQV
WASHADEVVT LPGDFDRLAT SSICGNEAIA HKHLPIFGIQ WHPEVSHTFE GHRVFENFFS
ICTGQNKG