Database: SPTrEMBLEntry: TMOF_PSEME
LinkDB: TMOF_PSEME
Original site: TMOF_PSEME
ID TMOF_PSEME Reviewed; 326 AA.
AC Q03304;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 19-JAN-2010, entry version 60.
DE RecName: Full=Toluene-4-monooxygenase electron transfer component;
DE Includes:
DE RecName: Full=Ferredoxin;
DE Includes:
DE RecName: Full=Ferredoxin--NAD(+) reductase;
DE EC=1.18.1.3;
GN Name=tmoF;
OS Pseudomonas mendocina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-14.
RC STRAIN=KR1;
RX MEDLINE=93054339; PubMed=1429451;
RA Yen K.-M., Karl M.R.;
RT "Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1
RT gene cluster encoding toluene-4-monooxygenase.";
RL J. Bacteriol. 174:7253-7261(1992).
CC -!- FUNCTION: Electron transfer component of toluene 4-monooxygenase
CC complex.
CC -!- CATALYTIC ACTIVITY: Reduced ferredoxin + NAD(+) = oxidized
CC ferredoxin + NADH.
CC -!- COFACTOR: FAD.
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC -!- SUBUNIT: The multicomponent enzyme toluene-4-monooxygenase is
CC formed by the tmoA, tmoB, tmoC, tmoD, tmoE and tmoF polypeptides.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC dioxygenase ferredoxin reductase family.
CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR EMBL; M95045; AAA26004.1; -; Genomic_DNA.
DR PIR; A47016; A47016.
DR SMR; Q03304; 4-326.
DR BRENDA; 1.18.1.3; 1102.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; b-grasp_ferredoxin-like.
DR InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR InterPro; IPR001041; Ferredoxin.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR008333; OxRdtase_FAD-bd_dom.
DR InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR InterPro; IPR001221; Phe_hydroxylase.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase.
FT CHAIN 1 326 Toluene-4-monooxygenase electron transfer
FT component.
FT /FTId=PRO_0000167658.
FT DOMAIN 1 92 2Fe-2S ferredoxin-type.
FT DOMAIN 100 195 FAD-binding FR-type.
FT REGION 95 326 Ferredoxin-reductase.
FT METAL 36 36 Iron-sulfur (2Fe-2S) (By similarity).
FT METAL 41 41 Iron-sulfur (2Fe-2S) (By similarity).
FT METAL 44 44 Iron-sulfur (2Fe-2S) (By similarity).
FT METAL 76 76 Iron-sulfur (2Fe-2S) (By similarity).
SQ SEQUENCE 326 AA; 35983 MW; 17889D794FC092EE CRC64;
MFNIQSDDLL HHFEADSNDT LLSAALRAEL VFPYECNSGG CGACKIELLE GEVSNLWPDA
PGLAARELRK NRFLACQCKP LSDLKIKVIN RAEGRASHPP KRFSTRVVSK RFLSDEMFEL
RLEAEQKVVF SPGQYFMVDV PELGTRAYSA ANPVDGNTLT LIVKAVPNGK VSCALANETI
ETLQLDGPYG LSVLKTADET QSVFIAGGSG IAPMVSMVNT LIAQGYEKPI TVFYGSRLEA
ELEAAETLFG WKENLKLINV SSSVVGNSEK KYPTGYVHEI IPEYMEGLLG AEFYLCGPPQ
MINSVQKLLM IENKVPFEAI HFDRFF
//
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