ID C4LJD4_CORK4 Unreviewed; 104 AA.
AC C4LJD4;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=ckrop_1194 {ECO:0000313|EMBL:ACR17939.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR17939.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR17939.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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}.
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DR EMBL; CP001620; ACR17939.1; -; Genomic_DNA.
DR RefSeq; WP_012731826.1; NC_012704.1.
DR AlphaFoldDB; C4LJD4; -.
DR STRING; 645127.ckrop_1194; -.
DR KEGG; ckp:ckrop_1194; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_3_0_11; -.
DR OrthoDB; 3182027at2; -.
DR Proteomes; UP000001473; 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 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; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT DOMAIN 14..104
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT REGION 74..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 104 AA; 11668 MW; 29103C94E7EACD17 CRC64;
MTTAESDQSH DPVRLTAWVH GYVQDVGFRW WTRSQALELG LVGSATNYSD GRVLVCAEGE
RAPVTELLAR LREEPTSTNR PGSVDNVVES WEEPRGGYQT FETR
//
