C5C4_AMYOR
ID C5C4_AMYOR Reviewed; 406 AA.
AC Q8RN03;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cytochrome P450 165C4;
DE EC=1.14.-.-;
DE AltName: Full=Vancomycin biosynthesis protein OxyC;
GN Name=cyp165C4; Synonyms=oxyC;
OS Amycolatopsis orientalis (Nocardia orientalis).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=31958 {ECO:0000312|EMBL:AAL90879.1};
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=12888556; DOI=10.1074/jbc.m306486200;
RA Pylypenko O., Vitali F., Zerbe K., Robinson J.A., Schlichting I.;
RT "Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-
RT C coupling reaction during vancomycin biosynthesis.";
RL J. Biol. Chem. 278:46727-46733(2003).
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 Evidence={ECO:0000269|PubMed:12888556};
CC -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
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; AF486630; AAL90879.1; -; Genomic_DNA.
DR PDB; 1UED; X-ray; 1.90 A; A/B=1-406.
DR PDBsum; 1UED; -.
DR AlphaFoldDB; Q8RN03; -.
DR SMR; Q8RN03; -.
DR STRING; 1125971.ASJB01000062_gene4401; -.
DR eggNOG; COG2124; Bacteria.
DR UniPathway; UPA00162; -.
DR EvolutionaryTrace; Q8RN03; -.
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..406
FT /note="Cytochrome P450 165C4"
FT /id="PRO_0000052240"
FT BINDING 356
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:0000269|PubMed:12888556,
FT ECO:0007744|PDB:1UED"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1UED"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 118..142
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 189..212
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 232..263
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:1UED"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 359..376
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:1UED"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1UED"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1UED"
SQ SEQUENCE 406 AA; 45187 MW; 6C0E2EFA167A747A CRC64;
MGHDIDQVAP LLREPANFQL RTNCDPHEDN FGLRAHGPLV RIVGESSTQL GRDFVWQAHG
YEVVRRILGD HEHFTTRPQF TQSKSGAHVE AQFVGQISTY DPPEHTRLRK MLTPEFTVRR
IRRMEPAIQS LIDDRLDLLE AEGPSADLQG LFADPVGAHA LCELLGIPRD DQREFVRRIR
RNADLSRGLK ARAADSAAFN RYLDNLLARQ RADPDDGLLG MIVRDHGDNV TDEELKGLCT
ALILGGVETV AGMIGFGVLA LLDNPGQIEL LFESPEKAER VVNELVRYLS PVQAPNPRLA
IKDVVIDGQL IKAGDYVLCS ILMANRDEAL TPDPDVLDAN RAAVSDVGFG HGIHYCVGAA
LARSMLRMAY QTLWRRFPGL RLAVPIEEVK YRSAFVDCPD QVPVTW
