XYLA_PSEPU
ID XYLA_PSEPU Reviewed; 350 AA.
AC P21394;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Xylene 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=xylA;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid TOL pWW0.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 6-16.
RX PubMed=1999388; DOI=10.1128/jb.173.5.1690-1695.1991;
RA Suzuki M., Hayakawa T., Shaw J.P., Rekik M., Harayama S.;
RT "Primary structure of xylene monooxygenase: similarities to and differences
RT from the alkane hydroxylation system.";
RL J. Bacteriol. 173:1690-1695(1991).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1327782; DOI=10.1111/j.1432-1033.1992.tb17260.x;
RA Shaw J.P., Harayama S.;
RT "Purification and characterisation of the NADH:acceptor reductase component
RT of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas
RT putida mt-2.";
RL Eur. J. Biochem. 209:51-61(1992).
CC -!- FUNCTION: Oxidizes toluene and xylenes to (methyl)benzyl alcohols. The
CC enzyme has a broad specificity and also oxidizes (methyl)benzyl
CC alcohols to (methyl)benzaldehydes and indole to indoxyl.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- SUBUNIT: Composed of two subunits: XylA and XylM.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
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DR EMBL; M37480; AAA26027.1; -; Genomic_DNA.
DR EMBL; D63341; BAA09663.1; -; Genomic_DNA.
DR PIR; B37316; B37316.
DR RefSeq; NP_542886.1; NC_003350.1.
DR RefSeq; WP_011005929.1; NC_003350.1.
DR AlphaFoldDB; P21394; -.
DR SMR; P21394; -.
DR KEGG; ag:AAA26027; -.
DR BioCyc; MetaCyc:MON-2941; -.
DR BRENDA; 1.18.1.3; 5092.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
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; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase;
KW Plasmid.
FT CHAIN 1..350
FT /note="Xylene monooxygenase electron transfer component"
FT /id="PRO_0000167660"
FT DOMAIN 16..108
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 114..213
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 109..350
FT /note="Ferredoxin--NADH reductase"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 57
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 60
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 92
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ 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
