ID   XYLZ_PSEPU              Reviewed;         336 AA.
AC   P23101;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Toluate 1,2-dioxygenase 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=xylZ;
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].
RX   PubMed=1938949; DOI=10.1128/jb.173.23.7540-7548.1991;
RA   Harayama S., Rekik M., Bairoch A., Neidle E.L., Ornston L.N.;
RT   "Potential DNA slippage structures acquired during evolutionary divergence
RT   of Acinetobacter calcoaceticus chromosomal benABC and Pseudomonas putida
RT   TOL pWW0 plasmid xylXYZ, genes encoding benzoate dioxygenases.";
RL   J. Bacteriol. 173:7540-7548(1991).
CC   -!- FUNCTION: Electron transfer component of toluate 1,2-dioxygenase
CC       system.
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; Evidence={ECO:0000250};
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: This dioxygenase system consists of three proteins: the two
CC       subunits of the hydroxylase component (XylX and XylY), and an electron
CC       transfer component (XylZ).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       ferredoxin reductase family. {ECO:0000305}.
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DR   EMBL; M64747; AAA26049.1; -; Genomic_DNA.
DR   PIR; C41659; C41659.
DR   RefSeq; NP_542869.1; NC_003350.1.
DR   RefSeq; WP_011005912.1; NC_003350.1.
DR   AlphaFoldDB; P23101; -.
DR   SMR; P23101; -.
DR   KEGG; ag:AAA26049; -.
DR   BioCyc; MetaCyc:MON-2963; -.
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   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Iron;
KW   Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..336
FT                   /note="Toluate 1,2-dioxygenase electron transfer component"
FT                   /id="PRO_0000167659"
FT   DOMAIN          3..97
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          104..204
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          99..336
FT                   /note="Ferredoxin-reductase"
FT   BINDING         40
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         48
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         81
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   336 AA;  36220 MW;  2E74B6A2E2757CAB CRC64;
     MTHKVATDFE DGVTRFIDAN TGETVADAAY RQGINLPLDC RDGACGACKC FAESGRYSLG
     EEYIEDALSE AEAEQGYVLT CQMRAESDCV IRVPAASDVC KTQQAGYQAA ISNVRQLSES
     TIALSIKSAS LNQLAFLPGQ YVNLQVPGSD QTRAYSFSSL QKDGEVSFLI RKLPGGLMSS
     FLTSLAKVGD SVSLAGPLGA FYLREIKRPL LLLAGGTGLA PFTAMLEKIA EQGGEHPLHL
     IYGVTHDHDL VEMDKLEAFA ARIPNFSYSA CVASPDSAYP QKGYVTQYIE PKQLNGGEVD
     IYLCGPPPMV EAVSQYIRAQ GIQPANFYYE KFAASA