ID G7WMX3_METH6 Unreviewed; 164 AA.
AC G7WMX3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN OrderedLocusNames=Mhar_1170 {ECO:0000313|EMBL:AET64538.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET64538.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET64538.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET64538.1,
RC ECO:0000313|Proteomes:UP000005877};
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|RuleBase:RU004168}.
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DR EMBL; CP003117; AET64538.1; -; Genomic_DNA.
DR RefSeq; WP_014586723.1; NC_017527.1.
DR AlphaFoldDB; G7WMX3; -.
DR STRING; 1110509.Mhar_1170; -.
DR GeneID; 25395408; -.
DR KEGG; mhi:Mhar_1170; -.
DR PATRIC; fig|1110509.7.peg.1297; -.
DR HOGENOM; CLU_118416_0_0_2; -.
DR OrthoDB; 146788at2157; -.
DR Proteomes; UP000005877; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR Pfam; PF00708; Acylphosphatase; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Reference proteome {ECO:0000313|Proteomes:UP000005877}.
FT DOMAIN 2..96
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 164 AA; 18607 MW; A21167B4E416A41A CRC64;
MKIKALITGP MVQGVGYRIF LMHQAIIEGI ERFSALNVSD NAVVVLAEAE EDKISNLKEF
LLTHRPEHAQ VSEVRIEDFK GLVMTLQEAT ALSTVEQMDK AIPILISMNE RMGRMDEKMD
RMLEKQDETV DQVRGLREDL GTIHAGRMER MERDIAEIKA KIGL
//
