ID   C1331_XYLFT             Reviewed;         402 AA.
AC   Q87AX5;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Putative cytochrome P450 133B1;
DE            EC=1.14.-.-;
GN   Name=cyp133B1; OrderedLocusNames=PD_1688;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AE009442; AAO29526.1; -; Genomic_DNA.
DR   RefSeq; WP_011098211.1; NC_004556.1.
DR   AlphaFoldDB; Q87AX5; -.
DR   SMR; Q87AX5; -.
DR   GeneID; 93905525; -.
DR   KEGG; xft:PD_1688; -.
DR   HOGENOM; CLU_033716_2_0_6; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd20625; CYP164-like; 1.
DR   FunFam; 1.10.630.10:FF:000018; Cytochrome P450 monooxygenase; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR46696:SF1; CYTOCHROME P450 YJIB-RELATED; 1.
DR   PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..402
FT                   /note="Putative cytochrome P450 133B1"
FT                   /id="PRO_0000052289"
FT   BINDING         348
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  45000 MW;  2AA7F2678E3C466C CRC64;
     MKLTDLSNPA FLENPYPLYE TLRAQAPFVS IGPNALMTGR YSLVDSLLHN RNMGKKYIES
     IRLRYGDTAA DMPLFQAFSR MFITINPPAH THLRGLVMQA FTGRESESMR PLAIDTAHQL
     IDNFEQKPSV DLVAEFAFPF PMQIICKMMD VDIGDAVTLG MAVSKIAKVL DPSPMSADEL
     VHASTAYEEL AQYFTKLIEL RRTHPGTDLI SMFLRAEEDG EKLTHDEIVS NVIMLLIAGY
     ETTSNMIGNA LIALHRHPEQ LALLKSDLSL MPQAVSECLR YDGSVQFTMR AAMDDIEVEG
     ELVPRGTVVF LMLGAANRDP AQFTHPDQLD ITRKQGRLQS FGAGIHHCLG YRLALIELEC
     ALTTLFERLP HLRLAHLDAL NWNQRSNLRG VNTLIVDLHA KN
//