ID F6F0U8_SPHCR Unreviewed; 411 AA.
AC F6F0U8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Camphor 5-monooxygenase {ECO:0000313|EMBL:AEG51164.1};
DE EC=1.14.15.1 {ECO:0000313|EMBL:AEG51164.1};
GN ORFNames=Sphch_3574 {ECO:0000313|EMBL:AEG51164.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG51164.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG51164.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG51164.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 2 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP002799; AEG51164.1; -; Genomic_DNA.
DR AlphaFoldDB; F6F0U8; -.
DR STRING; 690566.Sphch_3574; -.
DR KEGG; sch:Sphch_3574; -.
DR HOGENOM; CLU_033716_0_1_5; -.
DR Proteomes; UP000007150; Chromosome 2.
DR GO; GO:0018683; F:camphor 5-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd11035; P450cam-like; 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:SF2; CYTOCHROME P450 130; 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 {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461, ECO:0000313|EMBL:AEG51164.1};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461,
KW ECO:0000313|EMBL:AEG51164.1}.
SQ SEQUENCE 411 AA; 46114 MW; 1AEEDF587402C2F1 CRC64;
MSADVTSMAE GGLAPRPDHV PADLVRDFNI YDVPGAAEDV QAAYAAIQQA NPDIFWTPHN
GGHWVATRGE DIMAMQRDYH HFSHKHIVLP PMPEGTQRQI PLEMDPPEHA RYRRPLMQSL
MPAVVGELES KVRDVAVEAI ERVLPQGECE FIEDFAKILP IHVFLELVDL PLSDKHRLLP
MAERSVRGRS AEIRLQAQQE MGGYLLGEIR ARRENPGQDL LSKLVNVNVG DGRISEMEAV
SYATLVLFGG LDTVAGMIGF IARFLAMNPG HRRQLVERLD DEAFVKHAIE EMIRRHGLAN
TARVIAEDFE YGGVYFRAGD RILPANLWVG LDERINENPL VVDFDRDRPV HAAFGNGPHA
CPGAVLARRE IRIFLQEWLS RIPDFHIKPD TKPVLATGMV NGVLRLDLCW P
//
