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p-cumate 2,3-dioxygenase system, large oxygenase component (EC 1.14.12.25) (Large terminal subunit of p-cumate dioxygenase) (p-cumate 2,3-dioxygenase large subunit) (p-cumate 2,3-dioxygenase subunit alpha)

 CMTAB_PSEPU             Reviewed;         434 AA.
Q51974;
22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 101.
RecName: Full=p-cumate 2,3-dioxygenase system, large oxygenase component {ECO:0000303|PubMed:8631713};
EC=1.14.12.25 {ECO:0000305|PubMed:845117};
AltName: Full=Large terminal subunit of p-cumate dioxygenase {ECO:0000303|PubMed:8631713};
AltName: Full=p-cumate 2,3-dioxygenase large subunit {ECO:0000303|PubMed:8631713};
AltName: Full=p-cumate 2,3-dioxygenase subunit alpha {ECO:0000303|PubMed:8631713};
Name=cmtAb {ECO:0000303|PubMed:8631713};
ORFNames=CBP06_10605 {ECO:0000312|EMBL:OUS88312.1};
Pseudomonas putida (Arthrobacter siderocapsulatus).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=303;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND SUBUNIT.
STRAIN=F1 {ECO:0000312|EMBL:AAB62285.1};
PubMed=8631713; DOI=10.1128/jb.178.5.1351-1362.1996;
Eaton R.W.;
"p-cumate catabolic pathway in Pseudomonas putida F1: cloning and
characterization of DNA carrying the cmt operon.";
J. Bacteriol. 178:1351-1362(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=F1 {ECO:0000312|EMBL:AAB62285.1};
PubMed=9150211;
Eaton R.W.;
"p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and
characterization of DNA encoding conversion of p-cymene to p-cumate.";
J. Bacteriol. 179:3171-3180(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
PubMed=10333523; DOI=10.1016/S0378-1119(99)00113-4;
Mosqueda G., Ramos-Gonzalez M.I., Ramos J.L.;
"Toluene metabolism by the solvent-tolerant Pseudomonas putida DOT-T1
strain, and its role in solvent impermeabilization.";
Gene 232:69-76(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
PubMed=10648517; DOI=10.1128/JB.182.4.937-943.2000;
Mosqueda G., Ramos J.L.;
"A set of genes encoding a second toluene efflux system in Pseudomonas
putida DOT-T1 is linked to the tod genes for toluene metabolism.";
J. Bacteriol. 182:937-943(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11160798;
Ohta Y., Maeda M., Kudo T.;
"Pseudomonas putida CE2010 can degrade biphenyl by a mosaic pathway
encoded by the tod operon and cmtE, which are identical to those of P.
putida F1 except for a single base difference in the operator-promoter
region of the cmt operon.";
Microbiology 147:31-41(2001).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
PubMed=11251828; DOI=10.1046/j.1365-2958.2001.02310.x;
Duque E., Segura A., Mosqueda G., Ramos J.L.;
"Global and cognate regulators control the expression of the organic
solvent efflux pumps TtgABC and TtgDEF of Pseudomonas putida.";
Mol. Microbiol. 39:1100-1106(2001).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=KL47 {ECO:0000312|EMBL:ABA10794.1};
PubMed=16728956;
Lee K., Ryu E.K., Choi K.S., Cho M.C., Jeong J.J., Choi E.N.,
Lee S.O., Yoon D.Y., Hwang I., Kim C.K.;
"Identification and expression of the cym, cmt, and tod catabolic
genes from Pseudomonas putida KL47: expression of the regulatory todST
genes as a factor for catabolic adaptation.";
J. Microbiol. 44:192-199(2006).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
Daniels C., Godoy P., Duque E., Molina-Henares M.A., de la Torre J.,
Del Arco J.M., Herrera C., Segura A., Guazzaroni M.E., Ferrer M.,
Ramos J.L.;
"Global regulation of food supply by Pseudomonas putida DOT-T1E.";
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UV4/95 {ECO:0000312|EMBL:OUS88312.1};
Skvortsov T., Hoering P., Allen C.C.R.;
"Pseudomonas putida UV495 draft genome.";
Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=PL;
PubMed=845117;
DeFrank J.J., Ribbons D.W.;
"p-cymene pathway in Pseudomonas putida: initial reactions.";
J. Bacteriol. 129:1356-1364(1977).
[11]
FUNCTION, AND SUBSTRATE SPECIFICITY.
PubMed=7592495;
Eaton R.W., Chapman P.J.;
"Formation of indigo and related compounds from indolecarboxylic acids
by aromatic acid-degrading bacteria: chromogenic reactions for cloning
genes encoding dioxygenases that act on aromatic acids.";
J. Bacteriol. 177:6983-6988(1995).
-!- FUNCTION: Component of the p-cumate 2,3-dioxygenase multicomponent
enzyme system which catalyzes the incorporation of both atoms of
molecular oxygen into p-cumate to form cis-2,3-dihydroxy-2,3-
dihydro-p-cumate. The alpha subunit has a catalytic role in the
holoenzyme. Also able to catalyze the cis-dihydroxylation of
indole-2-carboxylate and indole-3-carboxylate (PubMed:7592495).
{ECO:0000269|PubMed:7592495, ECO:0000269|PubMed:845117,
ECO:0000305|PubMed:8631713}.
-!- CATALYTIC ACTIVITY: p-cumate + NADH + O(2) = (2R,3S)-2,3-
dihydroxy-2,3-dihydro-p-cumate + NAD(+).
{ECO:0000305|PubMed:845117}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00628};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000250|UniProtKB:P0A110};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000250|UniProtKB:P0A110};
-!- PATHWAY: Aromatic compound metabolism; p-cumate degradation;
acetaldehyde and pyruvate from p-cumate.
{ECO:0000305|PubMed:8631713}.
-!- SUBUNIT: The p-cumate 2,3-dioxygenase multicomponent enzyme system
is composed of an electron transfer component and a dioxygenase
component (iron sulfur protein (ISP)). The electron transfer
component is composed of a ferredoxin reductase (CmtAa) and a
ferredoxin (CmtAd), and the dioxygenase component is formed of a
large alpha subunit (CmtAb) and a small beta subunit (CmtAc).
{ECO:0000305|PubMed:8631713}.
-!- INDUCTION: Induced by p-cumate and repressed by CymR.
{ECO:0000269|PubMed:9150211}.
-!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
dioxygenase alpha subunit family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U24215; AAB62285.1; -; Genomic_DNA.
EMBL; AB042508; BAB17771.1; -; Genomic_DNA.
EMBL; DQ157469; ABA10794.1; -; Genomic_DNA.
EMBL; GQ884177; ADI95383.1; -; Genomic_DNA.
EMBL; NHBC01000013; OUS88312.1; -; Genomic_DNA.
RefSeq; WP_012052617.1; NZ_NHBC01000013.1.
eggNOG; ENOG4105FUY; Bacteria.
eggNOG; COG4638; LUCA.
BioCyc; MetaCyc:MONOMER-342; -.
Proteomes; UP000195461; Unassembled WGS sequence.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
Gene3D; 2.102.10.10; -; 1.
InterPro; IPR017941; Rieske_2Fe-2S.
InterPro; IPR036922; Rieske_2Fe-2S_sf.
InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
InterPro; IPR001663; Rng_hydr_dOase-A.
Pfam; PF00355; Rieske; 1.
Pfam; PF00848; Ring_hydroxyl_A; 1.
PRINTS; PR00090; RNGDIOXGNASE.
SUPFAM; SSF50022; SSF50022; 1.
PROSITE; PS51296; RIESKE; 1.
PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
1: Evidence at protein level;
2Fe-2S; Aromatic hydrocarbons catabolism; Complete proteome;
Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
CHAIN 1 434 p-cumate 2,3-dioxygenase system, large
oxygenase component.
/FTId=PRO_0000442282.
DOMAIN 43 153 Rieske. {ECO:0000255|PROSITE-
ProRule:PRU00628}.
METAL 84 84 Iron-sulfur (2Fe-2S).
{ECO:0000250|UniProtKB:P0A110,
ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 86 86 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000250|UniProtKB:P0A110,
ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 104 104 Iron-sulfur (2Fe-2S).
{ECO:0000250|UniProtKB:P0A110,
ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 107 107 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000250|UniProtKB:P0A110,
ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 211 211 Iron. {ECO:0000250|UniProtKB:P0A110}.
METAL 216 216 Iron. {ECO:0000250|UniProtKB:P0A110}.
METAL 365 365 Iron. {ECO:0000250|UniProtKB:P0A110}.
SEQUENCE 434 AA; 48968 MW; 820ABF7E578F4BCC CRC64;
MNNDKNLVEI DDENLLFRVA RESFVSEEVL AEEYEKIFDR CWLYVGHTSE FKKPGDFVTR
TVARRNLLVT MGTDRTINAF FNTCPHRGAT VCRERSGNSK NFQCFYHGWV FGCDGNLKSQ
PGKERYCADF ITGGAGNLVP VPRFDIYAGF CFVSFNAEVE PLPDYLAGAK EYLELVSKYS
ESGMGITTGT QEYAIRANWK LLVENSIDGY HAVSTHASYL DYLKNINDGF SGAKLEGKST
DLGNGHAVIE FSAPWGRPIA SWVPIWGEEG KQEIDQIYAR LVELHGAEMA DRMAYKNRNL
LIFPNLIIND IMAITVRTFY PQAPNYMHVN GWSLAPNEES DWARKYRLSN FLEFLGPGGF
ATPDDVEALE SCQNGFSNYR LVPWSDISKG MGKETANYDD ELQMRAFWTR WNQFIGGAPT
PDSGVQYIPT IALA


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