ID   XYLX_PSEPU              Reviewed;         454 AA.
AC   P23099;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Toluate 1,2-dioxygenase subunit alpha;
DE            EC=1.14.12.-;
GN   Name=xylX;
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=1740120; DOI=10.1111/j.1432-1033.1992.tb16612.x;
RA   Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S.;
RT   "Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the
RT   Acinetobacter calcoaceticus chromosomal benD gene are members of the short-
RT   chain alcohol dehydrogenase superfamily.";
RL   Eur. J. Biochem. 204:113-120(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-454.
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC       Note=Binds 1 Fe cation. {ECO:0000305};
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
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       alpha subunit family. {ECO:0000305}.
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DR   EMBL; M64747; AAA26047.1; -; Genomic_DNA.
DR   PIR; S23482; A41659.
DR   RefSeq; NP_542871.1; NC_003350.1.
DR   RefSeq; WP_011005914.1; NC_003350.1.
DR   AlphaFoldDB; P23099; -.
DR   SMR; P23099; -.
DR   KEGG; ag:AAA26047; -.
DR   BioCyc; MetaCyc:MON-2961; -.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017639; Benzo_1-2-diOase_lsu.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   PANTHER; PTHR43756; PTHR43756; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   TIGRFAMs; TIGR03229; benzo_1_2_benA; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW   Metal-binding; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..454
FT                   /note="Toluate 1,2-dioxygenase subunit alpha"
FT                   /id="PRO_0000085060"
FT   DOMAIN          51..148
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         92
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         94
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         112
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         115
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         221
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  51898 MW;  F68D1C41E236C077 CRC64;
     MTMTMHLGLD YIDSLVEEDE NEGIYRCKRE MFTDPRLFDL EMKHIFEGNW IYLAHESQIP
     EKNDYYTTQM GRQPIFITRN KDGELNAFVN ACSHRGATLC RFRSGNKATH TCSFHGWTFS
     NSGKLLKVKD PKGAGYPDSF DCDGSHDLKK VARFASYRGF LFGSLREDVA PLEEFLGESR
     KVIDMVVDQS PEGLEVLRGS STYVYEGNWK VQVENGADGY HVSTVHWNYA ATQQQRKLRD
     AGDDIRAMTA SSWGGDGGGF YSFENGHQMV WARWGDPKNR PLFAERDRLA SEFGEARADW
     MIGVSRNLCL YPNLYLMDQF GSQLRITRPL SVDRTEITIY CIAPKGETPR RARRVRQYED
     FFNVSGMATP DDLEEFRACQ EGFAGGGMND MSRGAKHWIE GPDEGAKEID LHPKLSGVRS
     EDEGLFVMQH KYWQQQMIKA VKREQDRLIH AEGV