ID I7J9E4_METBM Unreviewed; 228 AA.
AC I7J9E4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN OrderedLocusNames=BN140_1660 {ECO:0000313|EMBL:CCJ36583.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ36583.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(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; HE964772; CCJ36583.1; -; Genomic_DNA.
DR RefSeq; WP_014867557.1; NC_018227.2.
DR AlphaFoldDB; I7J9E4; -.
DR GeneID; 13356031; -.
DR KEGG; mbg:BN140_1660; -.
DR PATRIC; fig|1201294.9.peg.1823; -.
DR HOGENOM; CLU_080336_0_0_2; -.
DR BioCyc; MBOU1201294:BN140_RS08295-MONOMER; -.
DR Proteomes; UP000009007; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR47268; ACYLPHOSPHATASE; 1.
DR PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007}.
FT DOMAIN 3..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 123..185
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 228 AA; 26500 MW; 15FD04CB3C313CF0 CRC64;
MKRFSAVAAG RVQRVGFREH VYRETFDKDI SGYVKNLDNG EVEIVAEGSE EDLRALVDRI
NIIRYPIAVK SFAIKWQEAT GEFTSFEIIR GDLQEELFER VDFAGTIMYQ TLENSELSLK
KQDQMLEKQD QGLQLQHTML DKQDQMLEKQ DRMLDKQDQM LDKQDQMLDK QDQMLDKQDQ
MLQIGVETKE EIVGLRKDTR KYLDDEFAEI KKELAAIKGA LARAGIQV
//
