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(S)-phenoxypropionate/alpha-ketoglutarate-dioxygenase (SdpA) (EC 1.14.11.43) ((S)-dichlorprop/(S)-mecoprop dioxygenase) (Alpha-ketoglutarate-dependent dioxygenase) (Dichlorprop/alpha-ketoglutarate-dioxygenase) (Mecoprop/alpha-ketoglutarate-dioxygenase)

 SDPA_DELAC              Reviewed;         292 AA.
P83309; Q67FS3;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
29-OCT-2014, sequence version 2.
27-SEP-2017, entry version 42.
RecName: Full=(S)-phenoxypropionate/alpha-ketoglutarate-dioxygenase {ECO:0000303|PubMed:12501996};
Short=SdpA {ECO:0000303|PubMed:12501996};
EC=1.14.11.43 {ECO:0000269|Ref.5};
AltName: Full=(S)-dichlorprop/(S)-mecoprop dioxygenase {ECO:0000303|PubMed:12501996};
AltName: Full=Alpha-ketoglutarate-dependent dioxygenase {ECO:0000303|PubMed:12501996};
AltName: Full=Dichlorprop/alpha-ketoglutarate-dioxygenase {ECO:0000303|PubMed:12501996};
AltName: Full=Mecoprop/alpha-ketoglutarate-dioxygenase {ECO:0000303|PubMed:12501996};
Name=sdpA {ECO:0000303|PubMed:12501996};
Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
Plasmid pMC1.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Comamonadaceae; Delftia.
NCBI_TaxID=80866;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MC1; PLASMID=pMC1;
PubMed=15345421; DOI=10.1128/AEM.70.9.5357-5365.2004;
Schleinitz K.M., Kleinsteuber S., Vallaeys T., Babel W.;
"Localization and characterization of two novel genes encoding
stereospecific dioxygenases catalyzing 2(2,4-
dichlorophenoxy)propionate cleavage in Delftia acidovorans MC1.";
Appl. Environ. Microbiol. 70:5357-5365(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MC1; PLASMID=pMC1;
Schleinitz K.M., Kleinsteuber S., Vallaeys T., Babel W.;
"Genetic background of enantiospecific 2,4-dichlorophenoxypropionate
cleavage in Delftia acidovorans MC1.";
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MC1; PLASMID=pMC1;
Schleinitz K.M., Vallaeys T., Kleinsteuber S.;
"Structural analysis of ISCR8, a subgroup of IS91-like elements.";
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 1-25; 100-106 AND 170-182, FUNCTION, AND SUBUNIT.
STRAIN=MC1;
PubMed=12501996; DOI=10.1078/0944-5013-00164;
Westendorf A., Benndorf D., Mueller R.H., Babel W.;
"The two enantiospecific dichlorprop/alpha-ketoglutarate-dioxygenases
from Delftia acidovorans MC1 -- protein and sequence data of RdpA and
SdpA.";
Microbiol. Res. 157:317-322(2002).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
ENZYME REGULATION, PATHWAY, AND SUBSTRATE SPECIFICITY.
STRAIN=MC1;
Westendorf A., Mueller R.H., Babel W.;
"Purification and characterisation of the enantiospecific dioxygenases
from Delftia acidovorans MC1 initiating the degradation of
phenoxypropionate and phenoxyacetate herbicides.";
Acta Biotechnol. 23:3-17(2003).
[6]
INDUCTION.
STRAIN=MC1;
PubMed=15073309; DOI=10.1099/mic.0.26774-0;
Benndorf D., Davidson I., Babel W.;
"Regulation of catabolic enzymes during long-term exposure of Delftia
acidovorans MC1 to chlorophenoxy herbicides.";
Microbiology 150:1005-1014(2004).
-!- FUNCTION: Involved in the degradation of the phenoxypropionate
herbicides. Catalyzes the enantiospecific cleavage of the ether
bond in the herbicid S-dichlorprop ((S)-2-(2,4-
dichlorophenoxy)propionate)(S-2,4-DP) and S-mecoprop ((S)-2-(4-
chloro-2-methylphenoxy)propionate)(S-2,4-MCPP). It can also accept
(RS)-2-(4-chlorophenoxy)propionate, (RS)-2-(m-
chlorophenoxy)propionate and phenoxyacetate derivatives such as
2,4-dichlorophenoxyacetate (2,4-D), however it can only accept 2-
oxoglutarate as oxygen acceptor. {ECO:0000269|Ref.5,
ECO:0000303|PubMed:12501996}.
-!- CATALYTIC ACTIVITY: (S)-2-(4-chloro-2-methylphenoxy)propanoate +
2-oxoglutarate + O(2) = 4-chloro-2-methylphenol + pyruvate +
succinate + CO(2). {ECO:0000269|Ref.5}.
-!- CATALYTIC ACTIVITY: (S)-(2,4-dichlorophenoxy)propanoate + 2-
oxoglutarate + O(2) = 2,4-dichlorophenol + pyruvate + succinate +
CO(2). {ECO:0000269|Ref.5}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|Ref.5};
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
Evidence={ECO:0000269|Ref.5};
-!- ENZYME REGULATION: Inhibited by divalent cations, most
significantly by copper and nickel, and by diethylpyrocarbonate
(DEPC). {ECO:0000269|Ref.5}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=11.5 uM for (RS)-2-(m-chlorophenoxy)propionate (at pH 6 and
25 degrees Celsius) {ECO:0000269|Ref.5};
KM=21.8 uM for S-2,4-MCPP (at pH 6 and 25 degrees Celsius)
{ECO:0000269|Ref.5};
KM=24.1 uM for alpha-ketoglutarate (at pH 6 and 25 degrees
Celsius) {ECO:0000269|Ref.5};
KM=49 uM for S-2,4-DP (at pH 6 and 25 degrees Celsius)
{ECO:0000269|Ref.5};
KM=68.3 uM for (RS)-2-(4-chlorophenoxy)propionate (at pH 6 and
25 degrees Celsius) {ECO:0000269|Ref.5};
KM=122.8 uM for 2,4-D (at pH 6 and 25 degrees Celsius)
{ECO:0000269|Ref.5};
Note=Kcat is 50 min(-1) for dioxygenase activity with S-2,4-DP
(at pH 6 and 25 degrees Celsius). Kcat is 46 min(-1) for
dioxygenase activity with S-2,4-MCPP (at pH 6 and 25 degrees
Celsius). Kcat is 36 min(-1) for dioxygenase activity with 2,4-D
(at pH 6 and 25 degrees Celsius). Kcat is 17 min(-1) for
dioxygenase activity with (RS)-2-(4-chlorophenoxy)propionate (at
pH 6 and 25 degrees Celsius). Kcat is 15 min(-1) for dioxygenase
activity with (RS)-2-(m-chlorophenoxy)propionate (at pH 6 and 25
degrees Celsius). Kcat is 1.7 min(-1) for dioxygenase activity
with alpha-ketoglutarate (at pH 6 and 25 degrees Celsius).
{ECO:0000269|Ref.5};
pH dependence:
Optimum pH is about 6. {ECO:0000269|Ref.5};
Temperature dependence:
Optimum temperature is 25 degrees Celsius. {ECO:0000269|Ref.5};
-!- PATHWAY: Xenobiotic degradation; 2-(2,4-dichlorophenoxy)propanoate
degradation. {ECO:0000305|Ref.5}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12501996}.
-!- INDUCTION: Repressed during growth on high concentrations of 2,4-
dichlorophenoxypropionic acid (2,4-DCPP).
{ECO:0000269|PubMed:15073309}.
-!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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EMBL; AY327575; AAP88277.1; -; Genomic_DNA.
ProteinModelPortal; P83309; -.
SMR; P83309; -.
KEGG; ag:AAP88277; -.
KO; K21728; -.
BRENDA; 1.14.11.43; 1586.
UniPathway; UPA00348; -.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR003819; TauD/TfdA-like.
Pfam; PF02668; TauD; 1.
1: Evidence at protein level;
Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
Oxidoreductase; Plasmid; Vitamin C.
CHAIN 1 292 (S)-phenoxypropionate/alpha-
ketoglutarate-dioxygenase.
/FTId=PRO_0000097650.
METAL 108 108 Iron; catalytic.
{ECO:0000250|UniProtKB:P37610}.
METAL 110 110 Iron; catalytic.
{ECO:0000250|UniProtKB:P37610}.
METAL 262 262 Iron; catalytic.
{ECO:0000250|UniProtKB:P37610}.
BINDING 135 135 2-oxoglutarate.
{ECO:0000250|UniProtKB:P37610}.
BINDING 247 247 2-oxoglutarate.
{ECO:0000250|UniProtKB:P37610}.
BINDING 273 273 2-oxoglutarate.
{ECO:0000250|UniProtKB:P37610}.
CONFLICT 105 105 M -> T (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 170 170 K -> G (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 292 AA; 31658 MW; 1E158CF1386B139F CRC64;
MQTTLQITPT GATLGATVTG VHLATLDDAG FAALHAAWLQ HALLIFPGQH LSNDQQITFA
KRFGAIERIG GGDIVAISNV KADGTVRQHS PAEWDDMMKV IVGNMAWHAD STYMPVMAQG
AVFSAEVVPA VGGRTCFADM RAAYDALDEA TRALVHQRSA RHSLVYSQSK LGHVQQAGSA
YIGYGMDTTA TPLRPLVKVH PETGRPSLLI GRHAHAIPGM DAAESERFLE GLVDWACQAP
RVHAHQWAAG DVVVWDNRCL LHRAEPWDFK LPRVMWHSRL AGRPETEGAA LV


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