ID   C5A3_AMYOR              Reviewed;         391 AA.
AC   Q8RN05;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Cytochrome P450 165A3;
DE            EC=1.14.-.-;
DE   AltName: Full=Vancomycin biosynthesis protein OxyA;
GN   Name=cyp165A3; Synonyms=oxyA;
OS   Amycolatopsis orientalis (Nocardia orientalis).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=31958 {ECO:0000312|EMBL:AAL90877.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12207020; DOI=10.1074/jbc.m206342200;
RA   Zerbe K., Pylypenko O., Vitali F., Zhang W., Rousett S., Heck M.,
RA   Vrijbloed J.W., Bischoff D., Bister B., Suessmuth R.D., Pelzer S.,
RA   Wohlleben W., Robinson J.A., Schlichting I.;
RT   "Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative
RT   phenol coupling reaction during vancomycin biosynthesis.";
RL   J. Biol. Chem. 277:47476-47485(2002).
CC   -!- FUNCTION: Involved in the coupling of aromatic side chains of the
CC       heptapeptide of vancomycin.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF486630; AAL90877.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RN05; -.
DR   SMR; Q8RN05; -.
DR   STRING; 1125971.ASJB01000062_gene4399; -.
DR   eggNOG; COG2124; Bacteria.
DR   UniPathway; UPA00162; -.
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   GO; GO:0033072; P:vancomycin biosynthetic process; IEA:UniProtKB-UniPathway.
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   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..391
FT                   /note="Cytochrome P450 165A3"
FT                   /id="PRO_0000052238"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         342
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   391 AA;  43829 MW;  CA62DA0611E03EE4 CRC64;
     MFEEKNALRG TEIHRRERFD PGPELRALMA EGRMSVMESE ESPGGRTGWL ATGYEETRQV
     LGSDKFSAKL LFGGTAAGRI WPGFLNQYDP PEHTRLRRMV ASAFTVRRMR DFRPRIEAVV
     KATLDDIEAT GGPVDFVPRF AWPIATTVIC DFLGIPRDDQ AELSRVLHAS RSERSGKRRV
     AAGNKYWTYM GQVAAKTRRD PGDDMFGAVV REHGDDITDA ELLGVAAFVM GASGDQVARF
     LSAGAWLMVE HPEQFAVLRD DPDSVPDWLN EVARYLTSDE KTTPRIALED VRIGDQLVKK
     GDAVTCSLLA SNRHRFPDPE DRFDITREKP SHVTFGHGIH HCLGRPLAEM VFRTAIPALA
     HRFPTLRLAE PDREIKLGPP PFDVEALLLD W