ACYP_ECOLI
ID ACYP_ECOLI Reviewed; 92 AA.
AC P0AB65; P75877; Q9R7Q1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acylphosphatase {ECO:0000255|HAMAP-Rule:MF_01450, ECO:0000303|PubMed:17021943, ECO:0000303|PubMed:17134700};
DE EC=3.6.1.7 {ECO:0000255|HAMAP-Rule:MF_01450, ECO:0000269|PubMed:17134700};
DE AltName: Full=Acylphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01450, ECO:0000305};
GN Name=yccX {ECO:0000255|HAMAP-Rule:MF_01450};
GN OrderedLocusNames=b0968, JW5131;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY,
RP DISULFIDE BOND, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-5.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=17134700; DOI=10.1016/j.febslet.2006.11.033;
RA Ramazzotti M., Parrini C., Stefani M., Manao G., Degl'Innocenti D.;
RT "The intrachain disulfide bridge is responsible of the unusual stability
RT properties of novel acylphosphatase from Escherichia coli.";
RL FEBS Lett. 580:6763-6768(2006).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=17021943; DOI=10.1007/s10858-006-9073-2;
RA Pagano K., Ramazzotti M., Viglino P., Esposito G., Degl'Innocenti D.,
RA Taddei N., Corazza A.;
RT "NMR solution structure of the acylphosphatase from Escherichia coli.";
RL J. Biomol. NMR 36:199-204(2006).
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:0000255|HAMAP-Rule:MF_01450,
CC ECO:0000269|PubMed:17134700};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for benzoylphosphate {ECO:0000269|PubMed:17134700};
CC pH dependence:
CC Optimum pH is 5.2-6.5. {ECO:0000269|PubMed:17134700};
CC Temperature dependence:
CC Thermostable. Retains 85-90 % of its activity after 3 hours of
CC incubation at 90 degrees Celsius. {ECO:0000269|PubMed:17134700};
CC -!- MISCELLANEOUS: Has a considerably reduced catalytic efficiency compared
CC to other mesophilic acylphosphatases. Shows a considerable resistance
CC against urea denaturation since the full enzymatic activity is
CC maintained in the presence of urea concentrations approaching 6.0 M and
CC that only a slight decreae of 10-15 % was observed with higher urea
CC concentrations. {ECO:0000269|PubMed:17134700}.
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000255|HAMAP-
CC Rule:MF_01450}.
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DR EMBL; U00096; AAC74054.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35733.2; -; Genomic_DNA.
DR PIR; G64837; G64837.
DR RefSeq; NP_415488.1; NC_000913.3.
DR RefSeq; WP_000048252.1; NZ_SSZK01000002.1.
DR PDB; 2GV1; NMR; -; A=1-92.
DR PDBsum; 2GV1; -.
DR AlphaFoldDB; P0AB65; -.
DR BMRB; P0AB65; -.
DR SMR; P0AB65; -.
DR BioGRID; 4260041; 6.
DR BioGRID; 849681; 3.
DR DIP; DIP-11502N; -.
DR IntAct; P0AB65; 4.
DR STRING; 511145.b0968; -.
DR jPOST; P0AB65; -.
DR PaxDb; P0AB65; -.
DR PRIDE; P0AB65; -.
DR EnsemblBacteria; AAC74054; AAC74054; b0968.
DR EnsemblBacteria; BAA35733; BAA35733; BAA35733.
DR GeneID; 60899857; -.
DR GeneID; 945304; -.
DR KEGG; ecj:JW5131; -.
DR KEGG; eco:b0968; -.
DR PATRIC; fig|1411691.4.peg.1305; -.
DR EchoBASE; EB3490; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_1_2_6; -.
DR InParanoid; P0AB65; -.
DR OMA; VGFRWSM; -.
DR PhylomeDB; P0AB65; -.
DR BioCyc; EcoCyc:G6502-MON; -.
DR BioCyc; MetaCyc:G6502-MON; -.
DR BRENDA; 3.6.1.7; 2026.
DR SABIO-RK; P0AB65; -.
DR EvolutionaryTrace; P0AB65; -.
DR PRO; PR:P0AB65; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR HAMAP; MF_01450; Acylphosphatase_entero; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR028627; Acylphosphatase_bac.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR PANTHER; PTHR47268; PTHR47268; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Reference proteome.
FT CHAIN 1..92
FT /note="Acylphosphatase"
FT /id="PRO_0000158553"
FT DOMAIN 5..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT ACT_SITE 38
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT DISULFID 5..49
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01450,
FT ECO:0000269|PubMed:17134700"
FT MUTAGEN 5
FT /note="C->A: No change in secondary structure. Nearly
FT identical enzymatic properties. Loss of activity in 8.0 M
FT urea. Reduced thermodynamic activity. Inactivated after 3
FT hours of incubation at 90 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:17134700"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:2GV1"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:2GV1"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:2GV1"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2GV1"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2GV1"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2GV1"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:2GV1"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:2GV1"
SQ SEQUENCE 92 AA; 10300 MW; C39D3D145598D873 CRC64;
MSKVCIIAWV YGRVQGVGFR YTTQYEAKRL GLTGYAKNLD DGSVEVVACG EEGQVEKLMQ
WLKSGGPRSA RVERVLSEPH HPSGELTDFR IR
