CMTAB_PSEPU
ID CMTAB_PSEPU Reviewed; 434 AA.
AC Q51974;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=p-cumate 2,3-dioxygenase system, large oxygenase component {ECO:0000303|PubMed:8631713};
DE EC=1.14.12.25 {ECO:0000305|PubMed:845117};
DE AltName: Full=Large terminal subunit of p-cumate dioxygenase {ECO:0000303|PubMed:8631713};
DE AltName: Full=p-cumate 2,3-dioxygenase large subunit {ECO:0000303|PubMed:8631713};
DE AltName: Full=p-cumate 2,3-dioxygenase subunit alpha {ECO:0000303|PubMed:8631713};
GN Name=cmtAb {ECO:0000303|PubMed:8631713};
GN ORFNames=CBP06_10605 {ECO:0000312|EMBL:OUS88312.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=F1 {ECO:0000312|EMBL:AAB62285.1};
RX PubMed=8631713; DOI=10.1128/jb.178.5.1351-1362.1996;
RA Eaton R.W.;
RT "p-cumate catabolic pathway in Pseudomonas putida F1: cloning and
RT characterization of DNA carrying the cmt operon.";
RL J. Bacteriol. 178:1351-1362(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=F1 {ECO:0000312|EMBL:AAB62285.1};
RX PubMed=9150211; DOI=10.1128/jb.179.10.3171-3180.1997;
RA Eaton R.W.;
RT "p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and
RT characterization of DNA encoding conversion of p-cymene to p-cumate.";
RL J. Bacteriol. 179:3171-3180(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
RX PubMed=10333523; DOI=10.1016/s0378-1119(99)00113-4;
RA Mosqueda G., Ramos-Gonzalez M.I., Ramos J.L.;
RT "Toluene metabolism by the solvent-tolerant Pseudomonas putida DOT-T1
RT strain, and its role in solvent impermeabilization.";
RL Gene 232:69-76(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
RX PubMed=10648517; DOI=10.1128/jb.182.4.937-943.2000;
RA Mosqueda G., Ramos J.L.;
RT "A set of genes encoding a second toluene efflux system in Pseudomonas
RT putida DOT-T1 is linked to the tod genes for toluene metabolism.";
RL J. Bacteriol. 182:937-943(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11160798; DOI=10.1099/00221287-147-1-31;
RA Ohta Y., Maeda M., Kudo T.;
RT "Pseudomonas putida CE2010 can degrade biphenyl by a mosaic pathway encoded
RT by the tod operon and cmtE, which are identical to those of P. putida F1
RT except for a single base difference in the operator-promoter region of the
RT cmt operon.";
RL Microbiology 147:31-41(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
RX PubMed=11251828; DOI=10.1046/j.1365-2958.2001.02310.x;
RA Duque E., Segura A., Mosqueda G., Ramos J.L.;
RT "Global and cognate regulators control the expression of the organic
RT solvent efflux pumps TtgABC and TtgDEF of Pseudomonas putida.";
RL Mol. Microbiol. 39:1100-1106(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KL47 {ECO:0000312|EMBL:ABA10794.1};
RX PubMed=16728956;
RA Lee K., Ryu E.K., Choi K.S., Cho M.C., Jeong J.J., Choi E.N., Lee S.O.,
RA Yoon D.Y., Hwang I., Kim C.K.;
RT "Identification and expression of the cym, cmt, and tod catabolic genes
RT from Pseudomonas putida KL47: expression of the regulatory todST genes as a
RT factor for catabolic adaptation.";
RL J. Microbiol. 44:192-199(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DOT-T1E {ECO:0000312|EMBL:ADI95383.1};
RA Daniels C., Godoy P., Duque E., Molina-Henares M.A., de la Torre J.,
RA Del Arco J.M., Herrera C., Segura A., Guazzaroni M.E., Ferrer M.,
RA Ramos J.L.;
RT "Global regulation of food supply by Pseudomonas putida DOT-T1E.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV4/95 {ECO:0000312|EMBL:OUS88312.1};
RA Skvortsov T., Hoering P., Allen C.C.R.;
RT "Pseudomonas putida UV495 draft genome.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=PL;
RX PubMed=845117; DOI=10.1128/jb.129.3.1356-1364.1977;
RA DeFrank J.J., Ribbons D.W.;
RT "p-cymene pathway in Pseudomonas putida: initial reactions.";
RL J. Bacteriol. 129:1356-1364(1977).
RN [11]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=7592495; DOI=10.1128/jb.177.23.6983-6988.1995;
RA Eaton R.W., Chapman P.J.;
RT "Formation of indigo and related compounds from indolecarboxylic acids by
RT aromatic acid-degrading bacteria: chromogenic reactions for cloning genes
RT encoding dioxygenases that act on aromatic acids.";
RL J. Bacteriol. 177:6983-6988(1995).
CC -!- FUNCTION: Component of the p-cumate 2,3-dioxygenase multicomponent
CC enzyme system which catalyzes the incorporation of both atoms of
CC molecular oxygen into p-cumate to form cis-2,3-dihydroxy-2,3-dihydro-p-
CC cumate. The alpha subunit has a catalytic role in the holoenzyme. Also
CC able to catalyze the cis-dihydroxylation of indole-2-carboxylate and
CC indole-3-carboxylate (PubMed:7592495). {ECO:0000269|PubMed:7592495,
CC ECO:0000269|PubMed:845117, ECO:0000305|PubMed:8631713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + p-cumate = (2R,3S)-2,3-dihydroxy-2,3-
CC dihydro-p-cumate + NAD(+); Xref=Rhea:RHEA:42344, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:25822, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58420; EC=1.14.12.25;
CC Evidence={ECO:0000305|PubMed:845117};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P0A110};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A110};
CC -!- PATHWAY: Aromatic compound metabolism; p-cumate degradation;
CC acetaldehyde and pyruvate from p-cumate. {ECO:0000305|PubMed:8631713}.
CC -!- SUBUNIT: The p-cumate 2,3-dioxygenase multicomponent enzyme system is
CC composed of an electron transfer component and a dioxygenase component
CC (iron sulfur protein (ISP)). The electron transfer component is
CC composed of a ferredoxin reductase (CmtAa) and a ferredoxin (CmtAd),
CC and the dioxygenase component is formed of a large alpha subunit
CC (CmtAb) and a small beta subunit (CmtAc). {ECO:0000305|PubMed:8631713}.
CC -!- INDUCTION: Induced by p-cumate and repressed by CymR.
CC {ECO:0000269|PubMed:9150211}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; U24215; AAB62285.1; -; Genomic_DNA.
DR EMBL; AB042508; BAB17771.1; -; Genomic_DNA.
DR EMBL; DQ157469; ABA10794.1; -; Genomic_DNA.
DR EMBL; GQ884177; ADI95383.1; -; Genomic_DNA.
DR EMBL; NHBC01000013; OUS88312.1; -; Genomic_DNA.
DR RefSeq; WP_012052617.1; NZ_NHBC01000013.1.
DR AlphaFoldDB; Q51974; -.
DR SMR; Q51974; -.
DR EnsemblBacteria; OUS88312; OUS88312; CBP06_10605.
DR BioCyc; MetaCyc:MON-342; -.
DR BRENDA; 1.14.12.25; 5092.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0018570; F:p-cumate 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..434
FT /note="p-cumate 2,3-dioxygenase system, large oxygenase
FT component"
FT /id="PRO_0000442282"
FT DOMAIN 43..153
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 84
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 365
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
SQ 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
