ID   Q51973_PSEPU            Unreviewed;       402 AA.
AC   Q51973;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   19-JAN-2010, entry version 62.
DE   SubName: Full=Ferredoxin reductase subunit of p-cumated dioxgenase;
DE   SubName: Full=P-cumate dioxygenase ferredoxin reductase subunit;
DE   SubName: Full=P-cumate dioxygenase reductase component;
GN   Name=cmtAa;
OS   Pseudomonas putida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F1;
RX   MEDLINE=96200106; PubMed=8631713;
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.
RC   STRAIN=F1;
RX   MEDLINE=97294455; PubMed=9150211;
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.
RC   STRAIN=KL47;
RX   PubMed=16728956;
RA   Lee K., Ryu E.K., Choi K.S., Cho M.C., Jeong J.J., Choi E.N.,
RA   Lee S.O., Yoon D.Y., Hwang I., Kim C.K.;
RT   "Identification and expression of the cym, cmt, and tod catabolic
RT   genes from Pseudomonas putida KL47: expression of the regulatory todST
RT   genes as a factor for catabolic adaptation.";
RL   J. Microbiol. 44:192-199(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21097241; PubMed=11160798;
RA   Ohta Y., Maeda M., Kudo T.;
RT   "Pseudomonas putida CE2010 can degrade biphenyl by a mosaic pathway
RT   encoded by the tod operon and cmtE, which are identical to those of P.
RT   putida F1 except for a single base difference in the operator-promoter
RT   region of the cmt operon.";
RL   Microbiology 147:31-41(2001).
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DR   EMBL; U24215; AAB62284.1; -; Genomic_DNA.
DR   EMBL; DQ157469; ABA10793.1; -; Genomic_DNA.
DR   EMBL; AB042508; BAB17770.1; -; Genomic_DNA.
DR   HSSP; P16640; 1Q1W.
DR   SMR; Q51973; 6-401.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
PE   4: Predicted;
KW   Dioxygenase.
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
//