ID C1D9R9_LARHH Unreviewed; 94 AA.
AC C1D9R9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=LHK_02187 {ECO:0000313|EMBL:ACO75171.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO75171.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO75171.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO75171.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO75171.1; -; Genomic_DNA.
DR RefSeq; WP_012697657.1; NC_012559.1.
DR AlphaFoldDB; C1D9R9; -.
DR STRING; 557598.LHK_02187; -.
DR KEGG; lhk:LHK_02187; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_3_1_4; -.
DR Proteomes; UP000002010; 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 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; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520,
KW ECO:0000313|EMBL:ACO75171.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010}.
FT DOMAIN 3..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 94 AA; 10329 MW; C5F3A4F1704ABFDA CRC64;
MASKLLRIHG KVQGVYYRDN TVAMARAAGV AGWVRNRSDG TVEALIEGSA EQLERMLAWA
HRGPEAARVD RIDISEGHQA GEPVCMPFDR LPTL
//
