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Database: UniProt
Entry: W5W751_9PSEU
LinkDB: W5W751_9PSEU
Original site: W5W751_9PSEU 
ID   W5W751_9PSEU            Unreviewed;       416 AA.
AC   W5W751;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Cytochrome P450 107B1 {ECO:0000313|EMBL:AHH94039.1};
DE            EC=1.14.-.- {ECO:0000313|EMBL:AHH94039.1};
GN   ORFNames=KALB_664 {ECO:0000313|EMBL:AHH94039.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH94039.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH94039.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH94039.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; CP007155; AHH94039.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5W751; -.
DR   STRING; 1449976.KALB_664; -.
DR   KEGG; kal:KALB_664; -.
DR   PATRIC; fig|1449976.3.peg.675; -.
DR   eggNOG; COG2124; Bacteria.
DR   HOGENOM; CLU_033716_1_0_11; -.
DR   OrthoDB; 3665617at2; -.
DR   Proteomes; UP000019225; Chromosome.
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; cd11029; CYP107-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; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
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   ECO:0000313|EMBL:AHH94039.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019225}.
SQ   SEQUENCE   416 AA;  45310 MW;  D631431558371503 CRC64;
     MAATSSAGDP VRVPEPLLPA ARACPASGSA AAVGPAHRGR LVTGIESWLV TRYEEVAAAL
     SDPRLVMSAP RIQQELVDRG ALPERFGSLV QRRTRTLLST DPPEHSQLRR LVNPSFSGRT
     VDLLRERARQ VCGDLLAAMR ERSRQGEVVD LVDEFAFPLS VTMICQLLGA PAEDRERFRE
     WSQAIVFDHG DAESVAAYQR AMAAMDEYFG ELIAAKRAAP AEDLVSQLVA ADDERGGEDP
     AELRSMLSLL MIAGHETTAN LIASGVLELL RNPEQLAALR ADPGLLNPTV EECLRHAGPV
     AFSSMRFTTE EIRFGEVLVP RGEVVSLGLW AADHDPAHFP DPDAFDVHRR GDPHLAFGRG
     AHFCVGANLA RMQAQVALGT LLDSFGEIKL AVPEEELSWR PANTRGPRHL PLRLTE
//
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