CMTAC_PSEPU
ID CMTAC_PSEPU Reviewed; 180 AA.
AC Q51975;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=p-cumate 2,3-dioxygenase system, small oxygenase component {ECO:0000303|PubMed:8631713};
DE AltName: Full=Small terminal subunit of p-cumate dioxygenase {ECO:0000303|PubMed:8631713};
DE AltName: Full=p-cumate 2,3-dioxygenase small subunit {ECO:0000303|PubMed:8631713};
DE AltName: Full=p-cumate 2,3-dioxygenase subunit beta {ECO:0000303|PubMed:8631713};
GN Name=cmtAc {ECO:0000303|PubMed:8631713};
GN ORFNames=CBP06_10600 {ECO:0000312|EMBL:OUS88311.1};
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:AAB62286.1};
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:AAB62286.1};
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:ADI95384.1};
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:ADI95384.1};
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:ADI95384.1};
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:ABA10795.1};
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:ADI95384.1};
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:OUS88311.1};
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.
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 beta subunit seems to have a structural role in the
CC holoenzyme. Also able to catalyze the cis-dihydroxylation of indole-2-
CC carboxylate and indole-3-carboxylate (PubMed:7592495).
CC {ECO:0000269|PubMed:7592495, ECO:0000269|PubMed:845117,
CC ECO:0000305|PubMed:8631713}.
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 beta subunit family. {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; U24215; AAB62286.1; -; Genomic_DNA.
DR EMBL; GQ884177; ADI95384.1; -; Genomic_DNA.
DR EMBL; DQ157469; ABA10795.1; -; Genomic_DNA.
DR EMBL; AB042508; BAB17772.1; -; Genomic_DNA.
DR EMBL; NHBC01000013; OUS88311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q51975; -.
DR SMR; Q51975; -.
DR EnsemblBacteria; OUS88311; OUS88311; CBP06_10600.
DR BioCyc; MetaCyc:MON-346; -.
DR BRENDA; 1.14.12.25; 5092.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR PANTHER; PTHR41534; PTHR41534; 1.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Oxidoreductase.
FT CHAIN 1..180
FT /note="p-cumate 2,3-dioxygenase system, small oxygenase
FT component"
FT /id="PRO_0000442283"
SQ SEQUENCE 180 AA; 20734 MW; 77B2C4F8CAD9E67D CRC64;
MSAVALEKEP LRIPSSQDFA AFVTRSEVED LLYHEAELLD TWHLHDWLAL FTEDCSYFVP
STDLPRTASA DDSLFYIADD AVRLRERVIR LMKKTAHAEY PRSRTRHLVS NIRILAANAE
EIQVASAFVT YRMKLGNSDA YVGSTHYRLR RIDGQLRIVE KRCFLDLEAL RPHGRVSIIL
