ACYP_VIBC3
ID ACYP_VIBC3 Reviewed; 91 AA.
AC A5F8G9; C3M0B6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=VC0395_A0969, VC395_1474;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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 -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active site Arg in position 20. There is a
CC cysteine in this position. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ21959.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACP09482.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000627; ABQ21959.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001235; ACP09482.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000414764.1; NZ_JAACZH010000002.1.
DR PDB; 4HI1; X-ray; 1.96 A; A/B/C=1-91.
DR PDB; 4HI2; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-91.
DR PDB; 6KRB; X-ray; 2.38 A; A/B/C/D/E/F/G/H/I/J/K/L=1-91.
DR PDBsum; 4HI1; -.
DR PDBsum; 4HI2; -.
DR PDBsum; 6KRB; -.
DR AlphaFoldDB; A5F8G9; -.
DR SMR; A5F8G9; -.
DR STRING; 345073.VC395_1474; -.
DR EnsemblBacteria; ABQ21959; ABQ21959; VC0395_A0969.
DR KEGG; vco:VC0395_A0969; -.
DR KEGG; vcr:VC395_1474; -.
DR PATRIC; fig|345073.21.peg.1428; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_1_2_6; -.
DR BRENDA; 3.6.1.7; 6626.
DR Proteomes; UP000000249; Chromosome 2.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
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; PTHR47268; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase.
FT CHAIN 1..91
FT /note="Acylphosphatase"
FT /id="PRO_0000326840"
FT DOMAIN 5..91
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:4HI1"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:4HI1"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:4HI1"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:4HI1"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4HI1"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:4HI1"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:4HI1"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:4HI1"
SQ SEQUENCE 91 AA; 10226 MW; 40A67A424AB36C66 CRC64;
MEKQCSKFIV SGHVQGVGFC YHTSHQGLKL GLTGYAKNLN NGDVEVVACG TPERLEELYL
WLQEGPKTAS VRQVRRLSSE LEHDYQGFEI L
