ID   FAS1_RHOFA              Reviewed;         399 AA.
AC   P46373;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cytochrome P450 FAS1;
DE            EC=1.14.-.-;
GN   Name=fas1; Synonyms=CYP105E1;
OS   Rhodococcus fascians.
OG   Plasmid pFiD188.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=8169198; DOI=10.1128/jb.176.9.2492-2501.1994;
RA   Crespi M., Vereecke D., Temmerman W., van Montagu M., Desomer J.;
RT   "The fas operon of Rhodococcus fascians encodes new genes required for
RT   efficient fasciation of host plants.";
RL   J. Bacteriol. 176:2492-2501(1994).
CC   -!- FUNCTION: May be involved in the biosynthesis of cytokinin
CC       phytohormones and in host plant fasciation (leafy gall).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: During the interaction with host plants.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z29635; CAA82741.1; -; Genomic_DNA.
DR   PIR; A55578; A55578.
DR   RefSeq; WP_015586131.1; NZ_NPFU01000019.1.
DR   RefSeq; YP_007878704.1; NC_021080.1.
DR   AlphaFoldDB; P46373; -.
DR   SMR; P46373; -.
DR   STRING; 1443905.GCA_000761075_00040; -.
DR   GeneID; 29801291; -.
DR   eggNOG; COG2124; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Plasmid.
FT   CHAIN           1..399
FT                   /note="Cytochrome P450 FAS1"
FT                   /id="PRO_0000052231"
FT   BINDING         349
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   399 AA;  43596 MW;  A66B6F3DF1286566 CRC64;
     MAGTADLPLE MRRNGLNPTE ELAQVRDRDG VIPVGELYGA PAFLVCRYED VRRIFADSNR
     FSNAHTPMFA IPSGGDVIED ELAAMRAGNL IGLDPPDHTR LRHILAAEFS VHRLSRLQPR
     IAEIVDSALD GLEQAGQPAD LMDRYALPVS LLVLCELLGV PYADRDELRD RTARLLDLSA
     SAEQRAVAQR EDRRYMATLV TRAQEQPGDD LLGILARKIG DNLSTDELIS IISLIMLGGH
     ETTASMIGLS VLALLHHPEQ AAMMIEDPNC VNSGIEELLR WLSVAHSQPP RMAVTEVQIA
     GVTIPAGSFV IPSLLAANRD SNLTDRPDDL DITRGVAGHL AFGHGVHFCL GHSLARMTLR
     TAVPAVLRRF PDLALSPSHD VRLRSASIVL GLEELQLTW