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TFDB_DELAC
ID   TFDB_DELAC              Reviewed;         586 AA.
AC   Q8KN28; Q93T15; Q9RP01;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 3.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=2,4-dichlorophenol 6-monooxygenase;
DE            EC=1.14.13.20;
DE   AltName: Full=2,4-dichlorophenol hydroxylase;
DE            Short=2,4-DCP hydroxylase;
GN   Name=tfdB;
OS   Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=80866 {ECO:0000312|EMBL:AAM76774.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P4a {ECO:0000312|EMBL:AAM76774.1};
RX   PubMed=12949179; DOI=10.1099/mic.0.26260-0;
RA   Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.;
RT   "A transposon encoding the complete 2,4-dichlorophenoxyacetic acid
RT   degradation pathway in the alkalitolerant strain Delftia acidovorans P4a.";
RL   Microbiology 149:2545-2556(2003).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-434.
RC   STRAIN=P4a {ECO:0000312|EMBL:AAM76774.1};
RA   Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.;
RT   "Development and application of PCR primers for the detection of the tfd
RT   genes in Delftia acidovorans P4a involved in the degradation of 2,4-D.";
RL   Acta Biotechnol. 21:321-331(2001).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-432.
RC   STRAIN=MC1 {ECO:0000312|EMBL:AAD55079.1};
RX   PubMed=11572451; DOI=10.1078/0944-5013-00089;
RA   Mueller R.H., Kleinsteuber S., Babel W.;
RT   "Physiological and genetic characteristics of two bacterial strains
RT   utilizing phenoxypropionate and phenoxyacetate herbicides.";
RL   Microbiol. Res. 156:121-131(2001).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-19.
RC   STRAIN=MC1;
RX   PubMed=15073309; DOI=10.1099/mic.0.26774-0;
RA   Benndorf D., Davidson I., Babel W.;
RT   "Regulation of catabolic enzymes during long-term exposure of Delftia
RT   acidovorans MC1 to chlorophenoxy herbicides.";
RL   Microbiology 150:1005-1014(2004).
CC   -!- FUNCTION: Transforms 2,4-dichlorophenol (2,4-DCP) into 3,5-
CC       dichlorocatechol. {ECO:0000250|UniProtKB:P27138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-dichlorophenol + H(+) + NADPH + O2 = 3,5-dichlorocatechol
CC         + H2O + NADP(+); Xref=Rhea:RHEA:20920, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15788,
CC         ChEBI:CHEBI:16738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.14.13.20; Evidence={ECO:0000250|UniProtKB:P27138};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P27138};
CC   -!- PATHWAY: Xenobiotic degradation; (2,4-dichlorophenoxy)acetate
CC       degradation.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P27138}.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AY078159; AAM76774.1; -; Genomic_DNA.
DR   EMBL; AF176242; AAD55079.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KN28; -.
DR   SMR; Q8KN28; -.
DR   UniPathway; UPA00685; -.
DR   GO; GO:0018666; F:2,4-dichlorophenol 6-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0046300; P:2,4-dichlorophenoxyacetic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD;
KW   Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..586
FT                   /note="2,4-dichlorophenol 6-monooxygenase"
FT                   /id="PRO_0000214050"
FT   BINDING         11..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         304..314
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        2
FT                   /note="Missing (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="G -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="M -> V (in Ref. 3; AAD55079)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   586 AA;  64405 MW;  6BEE58517E7B860E CRC64;
     MNEKATVIET DVLVVGSGPA GAASTLLLAT YGVKTLCVSK YATTSRTPRS HITNQRTMEV
     MRDLGLELEC EAMASPAELM GENVYCTSLV GDELGRVLTW GTHPQRRADY ELASPTHMCD
     LPQNLLEPIM INHAARRGAD VRFHTEFVSL KQDETGVTAT VRDHLLDRQY DIRAKYLIGA
     DGANSQVVDQ VGLPMEGKMG VSGSINVVFE ADLTKYVGHR PSVLYWVIQP GSSVGGLGIG
     VIRMVRPWNK WLCIWGYDIA GGPPDLNEAH ARQIVHSLLG DSTIPVKIES TSTWTVNDMY
     ATRLFDNRVF CMGDAVHRHP PTNGLGSNTS IQDAFNLCWK LSHVLQGKAG PELLATYNEE
     RAPVARQVVQ RANKSLGDFP PILAALGLFD TKDPEQMQRN IARLKEQSPE AQEQRAALRA
     AIDGTQYVYN AHGVEMNQRY QSAAIVPDGT PDPGFRRDSE LYHAHSGRPG APVPHVWVTR
     HGRRVSTLDL CGKGRFSLLS GIAGSPWVEA AVHAAESLGI DLDVHIIGPG QELEDLYGDF
     ARVREIEESG ALLVRPDNFI CWRAMRWQEG SGDELRAALK RVLSVH
 
 
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