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Database: UniProt
Entry: C9KK26_9FIRM
LinkDB: C9KK26_9FIRM
Original site: C9KK26_9FIRM 
ID   C9KK26_9FIRM            Unreviewed;        96 AA.
AC   C9KK26;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|PROSITE-ProRule:PRU00520};
DE            EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN   ORFNames=MITSMUL_03524 {ECO:0000313|EMBL:EEX69476.1};
OS   Mitsuokella multacida DSM 20544.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Mitsuokella.
OX   NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX69476.1, ECO:0000313|Proteomes:UP000003671};
RN   [1] {ECO:0000313|EMBL:EEX69476.1, ECO:0000313|Proteomes:UP000003671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX69476.1,
RC   ECO:0000313|Proteomes:UP000003671};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) 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:EEX69476.1}.
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DR   EMBL; ABWK02000009; EEX69476.1; -; Genomic_DNA.
DR   RefSeq; WP_005839632.1; NZ_GG697141.2.
DR   AlphaFoldDB; C9KK26; -.
DR   STRING; 500635.MITSMUL_03524; -.
DR   GeneID; 78517202; -.
DR   PATRIC; fig|500635.8.peg.921; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_2_0_9; -.
DR   Proteomes; UP000003671; 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   PANTHER; PTHR47268; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
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   ECO:0000313|EMBL:EEX69476.1}.
FT   DOMAIN          9..96
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   96 AA;  10917 MW;  83E8382D59FD8429 CRC64;
     MAESTGIVRY FGRATGRVQG VGFRMFVQQH ASELGLTGWI RNMEDGSVEM EIQGDPAKVD
     KLSVLIREGN YFIKVKELKF EPIEAVSDET RFVVRY
//
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