位置:首页 > 蛋白库 > BPHD_DELAC
BPHD_DELAC
ID   BPHD_DELAC              Reviewed;         286 AA.
AC   Q8KRD3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase {ECO:0000255|HAMAP-Rule:MF_01688};
DE            Short=HOPDA hydrolase {ECO:0000255|HAMAP-Rule:MF_01688};
DE            EC=3.7.1.8 {ECO:0000255|HAMAP-Rule:MF_01688};
DE   AltName: Full=2,6-dioxo-6-phenylhexa-3-enoate hydrolase {ECO:0000255|HAMAP-Rule:MF_01688};
GN   Name=bphD {ECO:0000255|HAMAP-Rule:MF_01688};
OS   Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=80866;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SMN4;
RA   Lee N.-R., Min K.-H.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-
CC       6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-
CC       hydroxy-2,4-pentadienoic acid (HPD). {ECO:0000255|HAMAP-Rule:MF_01688}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,6-dioxo-6-phenylhexa-3-enoate + H2O = 2-oxopent-4-enoate +
CC         benzoate + H(+); Xref=Rhea:RHEA:17161, ChEBI:CHEBI:11641,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16150,
CC         ChEBI:CHEBI:64675; EC=3.7.1.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01688};
CC   -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC       pentadienoate and benzoate from biphenyl: step 4/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01688}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01688}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. BphD family.
CC       {ECO:0000255|HAMAP-Rule:MF_01688}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK31622.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY028943; AAK31622.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q8KRD3; -.
DR   SMR; Q8KRD3; -.
DR   ESTHER; delac-bphd; Carbon-carbon_bond_hydrolase.
DR   MEROPS; S33.016; -.
DR   UniPathway; UPA00155; UER00253.
DR   GO; GO:0018774; F:2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018771; F:2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01688; Biphenyl_BphD; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR017727; HOPD_hydrolase_BphD.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03343; biphenyl_bphD; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Hydrolase.
FT   CHAIN           1..286
FT                   /note="2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase"
FT                   /id="PRO_0000373812"
FT   DOMAIN          173..271
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT   BINDING         42..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT   SITE            112
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
SQ   SEQUENCE   286 AA;  31713 MW;  ACDBA4316991FD81 CRC64;
     MSELNESTTS KFVTINEKGL SNFRIHLNDA GEGEAVIMLH GGGPGAGGWS NYYRNIGPFV
     KAGYRVILKD APALNKSDTV VMHEQRGVVY ARSVKGMMHV LGIEEAHVVR KSMAGAGALN
     FALELPERTG KLILMGPGGL GNSLFTAMPM EGIKLLFKLY AEPSLDTLKQ MLNVFLFDQS
     LITDELVQGR WANIQRNPEH LKNFLLSAQK VPLSAWDVSP RLPEIKAKTL VTWGRDDRFV
     PLDHGLKLVA NMPDAQLHVF PRCVHWAQWE HADAFNRLTL DFLANG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024