ID   XYLM_PSEPU              Reviewed;         369 AA.
AC   P21395;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Xylene monooxygenase subunit 1;
DE            EC=1.14.15.-;
GN   Name=xylM;
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=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).
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   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 2 Fe(3+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Composed of two subunits: XylA and XylM.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M37480; AAA26026.1; -; Genomic_DNA.
DR   EMBL; D63341; BAA09662.1; -; Genomic_DNA.
DR   PIR; A37316; A37316.
DR   RefSeq; NP_542887.1; NC_003350.1.
DR   RefSeq; WP_011005930.1; NZ_QWEF01000005.1.
DR   AlphaFoldDB; P21395; -.
DR   PRIDE; P21395; -.
DR   KEGG; ag:AAA26026; -.
DR   BioCyc; MetaCyc:MON-2942; -.
DR   BRENDA; 1.14.15.26; 5092.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd03512; Alkane-hydroxylase; 1.
DR   InterPro; IPR033885; AlkB/XylM.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   PANTHER; PTHR38674; PTHR38674; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Cell inner membrane; Cell membrane;
KW   Membrane; Monooxygenase; Oxidoreductase; Plasmid; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..369
FT                   /note="Xylene monooxygenase subunit 1"
FT                   /id="PRO_0000185435"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   369 AA;  41566 MW;  AB76149B37DF7794 CRC64;
     MDTLRYYLIP VVTACGLIGF YYGGYWVWLG AATFPALMVL DVILPKDFSA RKVSPFFADL
     TQYLQLPLMI GLYGLLVFGV ENGRIELSEP LQVAGCILSL AWLSGVPTLP VSHELMHRRH
     WLPRKMAQLL AMFYGDPNRD IAHVNTHHLY LDTPLDSDTP YRGQTIYSFV ISATVGSVKD
     AIKIEAETLR RKGQSPWNLS NKTYQYVALL LALPGLVSYL GGPALGLVTI ASMIIAKGIV
     EGFNYFQHYG LVRDLDQPIL LHHAWNHMGT IVRPLGCEIT NHINHHIDGY TRFYELRPEK
     EAPQMPSLFV CFLLGLIPPL WFALIAKPKL RDWDQRYATP GERELAMAAN KKAGWPLWCE
     SELGRVASI