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Database: UniProt
Entry: A0A0J1BUZ1_9MICC
LinkDB: A0A0J1BUZ1_9MICC
Original site: A0A0J1BUZ1_9MICC 
ID   A0A0J1BUZ1_9MICC        Unreviewed;       436 AA.
AC   A0A0J1BUZ1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KLU10197.1};
GN   ORFNames=ABL57_08070 {ECO:0000313|EMBL:KLU10197.1};
OS   Kocuria sp. SM24M-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU10197.1, ECO:0000313|Proteomes:UP000036489};
RN   [1] {ECO:0000313|EMBL:KLU10197.1, ECO:0000313|Proteomes:UP000036489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU10197.1,
RC   ECO:0000313|Proteomes:UP000036489};
RA   Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA   Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA   Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA   Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT   "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KLU10197.1}.
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DR   EMBL; LDNX01000066; KLU10197.1; -; Genomic_DNA.
DR   RefSeq; WP_047802943.1; NZ_LDNX01000066.1.
DR   AlphaFoldDB; A0A0J1BUZ1; -.
DR   PATRIC; fig|1660349.3.peg.3705; -.
DR   OrthoDB; 54272at2; -.
DR   Proteomes; UP000036489; 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   CDD; cd00302; cytochrome_P450; 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; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46696:SF1; 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};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  48553 MW;  6D99EC1117277934 CRC64;
     MSDHDARCPV PHGDPSGDSH GDSHSDRRRT APPGERTTPR VEVRDGVWHV RALPLVRQVL
     READATVQAG FSAETARQGL TGDHPPVLYA DGPEHRRQRS ATAKFFTPAT VRRRYRDLME
     ERADELVERI RQDGGAELSA VTLRYSVEVA AQVVGLTNSD IDGMSRRLER FFSGPVTGSS
     GAPQRRLPGR LGAVVGAVRP VWAMSAFRLR DVRPAVRARR RQPREDVISH LLQQGYTDRE
     ILVECLTYAA AGMATTREFI AVAAWHLLED DGLRAEYLAA EEPARHGILH EILRLEPVVG
     HLYRRTTQDL VLEDGEERHE VPAGALLDLY VRQANADPQE LGEDARQLCP ERSRPKGVRP
     EVMSFGDGAH RCPGGFIAIQ ETDVFLQRLL RLPLEFAHPP RVSWVELIAA YEVRDVVLRV
     GAGQGWREPS PASTAR
//
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