C5B3_AMYOR
ID C5B3_AMYOR Reviewed; 398 AA.
AC Q8RN04;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cytochrome P450 165B3;
DE EC=1.14.-.-;
DE AltName: Full=Vancomycin biosynthesis protein OxyB;
GN Name=cyp165B3; Synonyms=oxyB;
OS Amycolatopsis orientalis (Nocardia orientalis).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=31958 {ECO:0000312|EMBL:AAL90878.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.7
RP ANGSTROMS).
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;
CC -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF486630; AAL90878.1; -; Genomic_DNA.
DR PDB; 1LFK; X-ray; 1.70 A; A=1-398.
DR PDB; 1LG9; X-ray; 2.00 A; A=1-398.
DR PDB; 1LGF; X-ray; 2.20 A; A=1-398.
DR PDBsum; 1LFK; -.
DR PDBsum; 1LG9; -.
DR PDBsum; 1LGF; -.
DR AlphaFoldDB; Q8RN04; -.
DR SMR; Q8RN04; -.
DR DIP; DIP-61594N; -.
DR IntAct; Q8RN04; 2.
DR STRING; 1125971.ASJB01000062_gene4400; -.
DR BindingDB; Q8RN04; -.
DR ChEMBL; CHEMBL1075039; -.
DR eggNOG; COG2124; Bacteria.
DR UniPathway; UPA00162; -.
DR EvolutionaryTrace; Q8RN04; -.
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 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT CHAIN 1..398
FT /note="Cytochrome P450 165B3"
FT /id="PRO_0000052239"
FT BINDING 347
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 HELIX 9..11
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1LFK"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1LG9"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1LFK"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 109..133
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1LFK"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 180..203
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 266..280
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:1LFK"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:1LFK"
FT TURN 323..326
FT /evidence="ECO:0007829|PDB:1LFK"
FT HELIX 350..367
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1LFK"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1LFK"
SQ SEQUENCE 398 AA; 44367 MW; F91FEA7FB0E91783 CRC64;
MSEDDPRPLH IRRQGLDPAD ELLAAGALTR VTIGSGADAE THWMATAHAV VRQVMGDHQQ
FSTRRRWDPR DEIGGKGIFR PRELVGNLMD YDPPEHTRLR RKLTPGFTLR KMQRMAPYIE
QIVNDRLDEM ERAGSPADLI AFVADKVPGA VLCELVGVPR DDRDMFMKLC HGHLDASLSQ
KRRAALGDKF SRYLLAMIAR ERKEPGEGMI GAVVAEYGDD ATDEELRGFC VQVMLAGDDN
ISGMIGLGVL AMLRHPEQID AFRGDEQSAQ RAVDELIRYL TVPYSPTPRI AREDLTLAGQ
EIKKGDSVIC SLPAANRDPA LAPDVDRLDV TREPIPHVAF GHGVHHCLGA ALARLELRTV
FTELWRRFPA LRLADPAQDT EFRLTTPAYG LTELMVAW
