ID D9XRK0_9ACTN Unreviewed; 355 AA.
AC D9XRK0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Cytochrome P450-SU2 {ECO:0000313|EMBL:EFL38625.1};
GN ORFNames=SSRG_01429 {ECO:0000313|EMBL:EFL38625.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL38625.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL38625.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL38625.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL Submitted (FEB-2009) 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; GG657758; EFL38625.1; -; Genomic_DNA.
DR AlphaFoldDB; D9XRK0; -.
DR STRING; 467200.SSRG_01429; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_1_1_11; -.
DR OrthoDB; 4133219at2; -.
DR Proteomes; UP000002968; 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; cd11030; CYP105-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}.
SQ SEQUENCE 355 AA; 39267 MW; D5C12B8334119BCB CRC64;
MVTRYDDVRE LLSDPRVSAD IRRPGFPALG EGEQEAGARF RPFIRTDAPE HTKYRRMLLP
VFTVRRVRAM RPAVQARVDE ILDGMLAGGG PVDFVSAYAN AVSTSVICEL LGIPRENLEF
FRDVTRVSGS RTSTAEQVSE ALGGLFGLLA ELVAKRREEP RDDLISKLVT EHLVPGHVTM
DQLLSTLGIT INAGRETTTS MISLSTLLLL DRPELMKELR REPSLMPAAV DEFLRVLSVA
DSIPLRVAAE DIDLSGRTIP ADDGVIALLA GANHDPEQFD DPERVDFHRT DNHHVAFGYG
VHQCVGQHLA RLELEVALET LIRRVPTLRL AGDRDDVAVK HDSATFGLEE LKVAW
//