ELH2_ACIAD
ID ELH2_ACIAD Reviewed; 267 AA.
AC P00632; Q43936;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=3-oxoadipate enol-lactonase 2;
DE EC=3.1.1.24;
DE AltName: Full=3-oxoadipate enol-lactonase II;
DE AltName: Full=Beta-ketoadipate enol-lactone hydrolase II;
DE AltName: Full=Enol-lactone hydrolase II;
GN Name=catD; OrderedLocusNames=ACIAD1451;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8125318; DOI=10.1016/0378-1119(94)90783-8;
RA Shanley M.S., Harrison A., Parales R.E., Kowalchuk G., Mitchell D.J.,
RA Ornston L.N.;
RT "Unusual G + C content and codon usage in catIJF, a segment of the ben-cat
RT supra-operonic cluster in the Acinetobacter calcoaceticus chromosome.";
RL Gene 138:59-65(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-30.
RX PubMed=670169; DOI=10.1016/s0021-9258(17)34635-5;
RA Yeh W.K., Davis G., Fletcher P., Ornston L.N.;
RT "Homologous amino acid sequences in enzymes mediating sequential metabolic
RT reactions.";
RL J. Biol. Chem. 253:4920-4923(1978).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O = 3-oxoadipate +
CC H(+); Xref=Rhea:RHEA:10184, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15775, ChEBI:CHEBI:58425; EC=3.1.1.24;
CC -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 3-
CC oxoadipate from 5-oxo-4,5-dihydro-2-furylacetate: step 1/1.
CC -!- MISCELLANEOUS: This species can form two 3-oxoadipate enol-lactonases
CC in response to different inducers. The one shown is called enol-lactone
CC hydrolase II by the authors.
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DR EMBL; AF009224; AAC46435.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68314.1; -; Genomic_DNA.
DR RefSeq; WP_004925432.1; NC_005966.1.
DR AlphaFoldDB; P00632; -.
DR SMR; P00632; -.
DR STRING; 62977.ACIAD1451; -.
DR ESTHER; acica-elh2; Carboxymethylbutenolide_lactonase.
DR EnsemblBacteria; CAG68314; CAG68314; ACIAD1451.
DR GeneID; 45233863; -.
DR KEGG; aci:ACIAD1451; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_020336_50_3_6; -.
DR OMA; MWRWQRE; -.
DR OrthoDB; 1196738at2; -.
DR BioCyc; ASP62977:ACIAD_RS06705-MON; -.
DR UniPathway; UPA00157; UER00261.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0047570; F:3-oxoadipate enol-lactonase activity; IEA:UniProtKB-EC.
DR GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR022742; Hydrolase_4.
DR InterPro; IPR026968; PcaD/CatD.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02427; protocat_pcaD; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; Hydrolase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:670169"
FT CHAIN 2..267
FT /note="3-oxoadipate enol-lactonase 2"
FT /id="PRO_0000086956"
FT CONFLICT 18
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29256 MW; 57B1E7DAED1C4A9D CRC64;
MPVFHFKDTL TAQDVALNYA TFGQADRPAL IFSNSLGTNL SMWQQQIAYF QDKYFVICYD
TRGHGASSTP VGPYRIDQLG TDVIALLDHL QIPQATFCGI SMGGLTGQWL AIHFPERFNQ
VIVANTAAKI GEAQAWQARA QLVREQGLTP IAQTAATRWF TPGFIEDSPE IVEKLSHDLA
QGSAEGYASC CEALAEADVR PQLQRISIPV LVIAGAQDPV TTVADGQFLC EHIVHSTLEV
LEASHISNVE QPQAFNHAVE AVMKRFN