ID M6EWC2_9LEPT Unreviewed; 95 AA.
AC M6EWC2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=LEP1GSC008_1215 {ECO:0000313|EMBL:EMK20783.1};
OS Leptospira kirschneri serovar Bulgarica str. Nikolaevo.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1240687 {ECO:0000313|EMBL:EMK20783.1, ECO:0000313|Proteomes:UP000011980};
RN [1] {ECO:0000313|EMBL:EMK20783.1, ECO:0000313|Proteomes:UP000011980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nikolaevo {ECO:0000313|EMBL:EMK20783.1,
RC ECO:0000313|Proteomes:UP000011980};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000744, ECO:0000256|PROSITE-
CC ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|RuleBase:RU004168}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMK20783.1}.
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DR EMBL; ANCE01000203; EMK20783.1; -; Genomic_DNA.
DR RefSeq; WP_000534971.1; NZ_ANCE01000203.1.
DR AlphaFoldDB; M6EWC2; -.
DR SMR; M6EWC2; -.
DR GeneID; 61143044; -.
DR PATRIC; fig|1240687.3.peg.4332; -.
DR OrthoDB; 9808093at2; -.
DR Proteomes; UP000011980; Unassembled WGS sequence.
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 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; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520}.
FT DOMAIN 8..95
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 23
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 95 AA; 10826 MW; FF690E8BA2C70A35 CRC64;
MGSKNNSRAK ILVRGKVQGV GFRYYILQRA QECRLSGYTQ NLPGGEVETV VEGDKMFIED
LYRAIQRGPK GSEVKEALIT WEDPKGNFRT FEIKK
//