CMTAA_PSEPU
ID CMTAA_PSEPU Reviewed; 402 AA.
AC Q51973;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=p-cumate 2,3-dioxygenase system, ferredoxin--NAD(+) reductase component {ECO:0000303|PubMed:8631713};
DE EC=1.18.1.3 {ECO:0000305|PubMed:8631713};
GN Name=cmtAa {ECO:0000303|PubMed:8631713};
GN ORFNames=CBP06_10610 {ECO:0000312|EMBL:OUS88313.1};
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, CATALYTIC ACTIVITY, COFACTOR,
RP PATHWAY, AND SUBUNIT.
RC STRAIN=F1 {ECO:0000312|EMBL:AAB62284.1};
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:AAB62284.1};
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KL47 {ECO:0000312|EMBL:ABA10793.1};
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV4/95 {ECO:0000312|EMBL:OUS88313.1};
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 [6]
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 [7]
RP FUNCTION.
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. Ferredoxin reductase catalyzes the transfer of electrons from
CC NADH to ferredoxin (CmtAd). {ECO:0000269|PubMed:7592495,
CC ECO:0000269|PubMed:845117, ECO:0000305|PubMed:8631713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3;
CC Evidence={ECO:0000305|PubMed:8631713};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={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 FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; U24215; AAB62284.1; -; Genomic_DNA.
DR EMBL; AB042508; BAB17770.1; -; Genomic_DNA.
DR EMBL; DQ157469; ABA10793.1; -; Genomic_DNA.
DR EMBL; NHBC01000013; OUS88313.1; -; Genomic_DNA.
DR RefSeq; WP_012052618.1; NZ_NHBC01000013.1.
DR AlphaFoldDB; Q51973; -.
DR SMR; Q51973; -.
DR EnsemblBacteria; OUS88313; OUS88313; CBP06_10610.
DR BioCyc; MetaCyc:MON-341; -.
DR BRENDA; 1.14.12.25; 5092.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..402
FT /note="p-cumate 2,3-dioxygenase system, ferredoxin--NAD(+)
FT reductase component"
FT /id="PRO_0000442281"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
SQ SEQUENCE 402 AA; 43178 MW; 38A0DB08536EABA6 CRC64;
MGEDISKIVI IGAGQAGATV AFGLRRNGFA GEITLVGEES HLPYERPQLS KEMLRPEASA
HKSIKTRADY EEQSILLELG CKVVRADAQA HSIVLDDGRQ LAFDRLVIAT GVQPRRLSSA
FQGAHRVHYL RTLEDAARLR ADLEAGKSLA IVGGGVIGLE VAAAARALNC PVTLIEAADR
LMSRSVDEVV SAYLDRAHRR NGVDIRYGVA ATELLDDGRL RLSDGGTVPA EAVLVGIGVT
PNIEGFEHLD ITDATGVRVD AYSQTVVPGI FATGDIASQP NGGGFGRIET WANAQDHALN
LVKNLMGEAV PYEAPVWFWS DQGPINLQVV GDAANGRRIV RGDEHGDVFS VFRLDANQQV
IGCATVNSPK DMAVARRWVK QRSSVDPQRL ADPTIPLRDC AV
