ID A9DPF5_9FLAO Unreviewed; 444 AA.
AC A9DPF5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Cytochrome P450 hydroxylase {ECO:0000313|EMBL:EDP97423.1};
GN ORFNames=KAOT1_19712 {ECO:0000313|EMBL:EDP97423.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP97423.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP97423.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP97423.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(2011).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP97423.1}.
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DR EMBL; ABIB01000002; EDP97423.1; -; Genomic_DNA.
DR RefSeq; WP_007096473.1; NZ_DS544873.1.
DR AlphaFoldDB; A9DPF5; -.
DR STRING; 391587.KAOT1_19712; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_001570_5_1_10; -.
DR OrthoDB; 9764248at2; -.
DR Proteomes; UP000002945; Unassembled WGS sequence.
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; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
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};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000002945}.
SQ SEQUENCE 444 AA; 51985 MW; E0B2E965010DDBFC CRC64;
MYNYPNTIPF FKLFLKSSSI TRNPIPFHKS GFEKHGNSFA IAPPFAKKVM LTRDAEITKH
LLRKNHRNYN KSKIQTKFLS KYVGKGLLTS SGDYWLKQRR LIQPAFHREK LQKLVAIMEG
TIEKQLENIQ RNKVIDSYPI MNELAFHVVA KSLFNYSSDD NTMHRLQEII ETLQDFIIRE
IRQPHKKWWY QISGLVKKHM ELVKESRDII NKVIDERRVS DKEHDDLLDM LLKAKYEDDG
TSMTNEQLID EILIFFVAGH ETTANALTFT FHLIARNSEV YKKVVAEIDT IDDGLPPMEK
IAKLNYVKNC VEEALRLYPP AWITDRVAIE DDEFAGFKIE KGTMIGISFY ELHRNPTYWK
NPNDFIPERF SDENRKETAG YYFPFGAGPR MCIGNSFALY EMMLTVYQML KKYRIETDQE
TVEIAPLITL KPINVTLKFN KRNA
//
