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Xylene monooxygenase electron transfer component [Includes: Ferredoxin; Ferredoxin--NAD( ) reductase (EC 1.18.1.3)]

 XYLA_PSEPU              Reviewed;         350 AA.
P21394;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
15-MAR-2017, entry version 98.
RecName: Full=Xylene monooxygenase electron transfer component;
Includes:
RecName: Full=Ferredoxin;
Includes:
RecName: Full=Ferredoxin--NAD(+) reductase;
EC=1.18.1.3;
Name=xylA;
Pseudomonas putida (Arthrobacter siderocapsulatus).
Plasmid TOL pWW0.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=303;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 6-16.
PubMed=1999388; DOI=10.1128/jb.173.5.1690-1695.1991;
Suzuki M., Hayakawa T., Shaw J.P., Rekik M., Harayama S.;
"Primary structure of xylene monooxygenase: similarities to and
differences from the alkane hydroxylation system.";
J. Bacteriol. 173:1690-1695(1991).
[2]
CHARACTERIZATION.
PubMed=1327782; DOI=10.1111/j.1432-1033.1992.tb17260.x;
Shaw J.P., Harayama S.;
"Purification and characterisation of the NADH:acceptor reductase
component of xylene monooxygenase encoded by the TOL plasmid pWW0 of
Pseudomonas putida mt-2.";
Eur. J. Biochem. 209:51-61(1992).
-!- FUNCTION: Oxidizes toluene and xylenes to (methyl)benzyl alcohols.
The enzyme has a broad specificity and also oxidizes
(methyl)benzyl alcohols to (methyl)benzaldehydes and indole to
indoxyl.
-!- CATALYTIC ACTIVITY: Reduced ferredoxin + NAD(+) = oxidized
ferredoxin + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
-!- SUBUNIT: Composed of two subunits: XylA and XylM.
-!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
dioxygenase ferredoxin reductase family. {ECO:0000305}.
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EMBL; M37480; AAA26027.1; -; Genomic_DNA.
EMBL; D63341; BAA09663.1; -; Genomic_DNA.
PIR; B37316; B37316.
RefSeq; NP_542886.1; NC_003350.1.
RefSeq; WP_011005929.1; NC_003350.1.
ProteinModelPortal; P21394; -.
SMR; P21394; -.
PRIDE; P21394; -.
GeneID; 1218743; -.
BioCyc; MetaCyc:MONOMER-2941; -.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
CDD; cd00207; fer2; 1.
Gene3D; 3.10.20.30; -; 1.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR012675; Beta-grasp_dom.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR008333; OxRdtase_FAD-bd_dom.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR001221; Phe_hydroxylase.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00970; FAD_binding_6; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00371; FPNCR.
PRINTS; PR00410; PHEHYDRXLASE.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing;
FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; NAD;
Oxidoreductase; Plasmid.
CHAIN 1 350 Xylene monooxygenase electron transfer
component.
/FTId=PRO_0000167660.
DOMAIN 16 108 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 114 213 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
REGION 109 350 Ferredoxin--NADH reductase.
METAL 52 52 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 57 57 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 60 60 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 92 92 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
SEQUENCE 350 AA; 38455 MW; 26828AC2226C1DDD CRC64;
MNEFFKKISG LFVPPPESTV SVRGQGFQFK VPRGQTILES ALHQGIAFPH DCKVGSCGTC
KYKLISGRVN ELTSSAMGLS GDLYQSGYRL GCQCIPKEDL EIELDTVLGQ ALVPIETSAL
ISKQKRLAHD IVEMEVVPDK QIAFYPGQYA DVECAECSAV RSYSFSAPPQ PDGSLSFHVR
LVPGGVFSGW LFGGDRTGAT LTLRAPYGQF GLHESNATMV CVAGGTGLAP IKCVLQSMTQ
AQRERDVLLF FGARQQRDLY CLDEIEALQL DWGGRFELIP VLSEESSTSS WKGKRGMVTE
YFKEYLTGQP YEGYLCGPPP MVDAAETELV RLGVARELVF ADRFYNRPPC


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