ID CYPE_BACSU Reviewed; 1054 AA. AC O08336; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 08-FEB-2011, entry version 96. DE RecName: Full=Probable bifunctional P-450/NADPH-P450 reductase 2; DE Includes: DE RecName: Full=Cytochrome P450 102; DE EC=1.14.14.1; DE Includes: DE RecName: Full=NADPH--cytochrome P450 reductase; DE EC=1.6.2.4; GN Name=cypE; Synonyms=CYP102A3, yrhJ; OrderedLocusNames=BSU27160; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=97453479; PubMed=9308178; RA Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J., RA Duesterhoeft A., Ehrlich S.D.; RT "Sequence of the Bacillus subtilis genome region in the vicinity of RT the lev operon reveals two new extracytoplasmic function RNA RT polymerase sigma factors SigV and SigZ."; RL Microbiology 143:2939-2943(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP INDUCTION. RX PubMed=11574077; RA Lee T.-R., Hsu H.-P., Shaw G.-C.; RT "Transcriptional regulation of the Bacillus subtilis bscR-CYP102A3 RT operon by the BscR repressor and differential induction of cytochrome RT CYP102A3 expression by oleic acid and palmitate."; RL J. Biochem. 130:569-574(2001). CC -!- FUNCTION: Functions as a fatty acid monooxygenase. The reductase CC domain is required for electron transfer from NADP to cytochrome CC P450 (By similarity). CC -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n CC reduced hemoprotein. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: FAD (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- INDUCTION: By palmitate and oleate. Negatively regulated by the CC transcriptional repressor BscR. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome CC P450 family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U93874; AAB80867.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14658.1; -; Genomic_DNA. DR PIR; A69975; A69975. DR RefSeq; NP_390594.1; NC_000964.3. DR ProteinModelPortal; O08336; -. DR SMR; O08336; 29-455, 478-1052. DR EnsemblBacteria; EBBACT00000001470; EBBACP00000001470; EBBACG00000001468. DR GeneID; 937585; -. DR GenomeReviews; AL009126_GR; BSU27160. DR KEGG; bsu:BSU27160; -. DR NMPDR; fig|224308.1.peg.2719; -. DR GenoList; BSU27160; -. DR GeneTree; EBGT00050000001044; -. DR HOGENOM; HBG334751; -. DR OMA; EDYPACE; -. DR PhylomeDB; O08336; -. DR ProtClustDB; CLSK886838; -. DR BioCyc; BSUB:BSU27160-MONOMER; -. DR BRENDA; 1.14.14.1; 150. DR BRENDA; 1.6.2.4; 150. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:EC. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR023206; Bifunctional_P450_P450_red. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR015702; Cyt_P450/sulfite_Rdtase/NOS. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1. DR Gene3D; G3DSA:1.20.990.10; NADPH_Cyt_P450_Rdtase_dom3; 1. DR PANTHER; PTHR19384:SF17; NADPH_Cyt_Red; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF48264; Cytochrome_P450; 1. DR SUPFAM; SSF63380; Riboflavin_synthase_like_b-brl; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Electron transport; FAD; Flavoprotein; KW FMN; Heme; Iron; Metal-binding; Monooxygenase; Multifunctional enzyme; KW NADP; Oxidoreductase; Transport. FT CHAIN 1 1054 Probable bifunctional P-450/NADPH-P450 FT reductase 2. FT /FTId=PRO_0000052207. FT DOMAIN 486 625 Flavodoxin-like. FT DOMAIN 663 896 FAD-binding FR-type. FT REGION 1 475 Cytochrome P450. FT REGION 472 1053 NADPH-P-450 reductase. FT METAL 403 403 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 1054 AA; 118676 MW; 705F8E27866CA110 CRC64; MKQASAIPQP KTYGPLKNLP HLEKEQLSQS LWRIADELGP IFRFDFPGVS SVFVSGHNLV AEVCDEKRFD KNLGKGLQKV REFGGDGLFT SWTHEPNWQK AHRILLPSFS QKAMKGYHSM MLDIATQLIQ KWSRLNPNEE IDVADDMTRL TLDTIGLCGF NYRFNSFYRD SQHPFITSML RALKEAMNQS KRLGLQDKMM VKTKLQFQKD IEVMNSLVDR MIAERKANPD ENIKDLLSLM LYAKDPVTGE TLDDENIRYQ IITFLIAGHE TTSGLLSFAI YCLLTHPEKL KKAQEEADRV LTDDTPEYKQ IQQLKYIRMV LNETLRLYPT APAFSLYAKE DTVLGGEYPI SKGQPVTVLI PKLHRDQNAW GPDAEDFRPE RFEDPSSIPH HAYKPFGNGQ RACIGMQFAL QEATMVLGLV LKHFELINHT GYELKIKEAL TIKPDDFKIT VKPRKTAAIN VQRKEQADIK AETKPKETKP KHGTPLLVLF GSNLGTAEGI AGELAAQGRQ MGFTAETAPL DDYIGKLPEE GAVVIVTASY NGAPPDNAAG FVEWLKELEE GQLKGVSYAV FGCGNRSWAS TYQRIPRLID DMMKAKGASR LTAIGEGDAA DDFESHRESW ENRFWKETMD AFDINEIAQK EDRPSLSITF LSEATETPVA KAYGAFEGIV LENRELQTAA STRSTRHIEL EIPAGKTYKE GDHIGILPKN SRELVQRVLS RFGLQSNHVI KVSGSAHMAH LPMDRPIKVV DLLSSYVELQ EPASRLQLRE LASYTVCPPH QKELEQLVSD DGIYKEQVLA KRLTMLDFLE DYPACEMPFE RFLALLPSLK PRYYSISSSP KVHANIVSMT VGVVKASAWS GRGEYRGVAS NYLAELNTGD AAACFIRTPQ SGFQMPNDPE TPMIMVGPGT GIAPFRGFIQ ARSVLKKEGS TLGEALLYFG CRRPDHDDLY REELDQAEQD GLVTIRRCYS RVENEPKGYV QHLLKQDTQK LMTLIEKGAH IYVCGDGSQM APDVERTLRL AYEAEKAASQ EESAVWLQKL QDQRRYVKDV WTGM //