true2000-12-012024-03-27169CYPB_BACSUSequence of the Bacillus subtilis genome region in the vicinity of the lev operon reveals two new extracytoplasmic function RNA polymerase sigma factors SigV and SigZ.Sorokin A.Bolotin A.Purnelle B.Hilbert H.Lauber J.Duesterhoeft A.Ehrlich S.D.doi:10.1099/00221287-143-9-29391997Microbiology1432939-2943NUCLEOTIDE SEQUENCE [GENOMIC DNA]168The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.Kunst F.Ogasawara N.Moszer I.Albertini A.M.Alloni G.Azevedo V.Bertero M.G.Bessieres P.Bolotin A.Borchert S.Borriss R.Boursier L.Brans A.Braun M.Brignell S.C.Bron S.Brouillet S.Bruschi C.V.Caldwell B.Capuano V.Carter N.M.Choi S.-K.Codani J.-J.Connerton I.F.Cummings N.J.Daniel R.A.Denizot F.Devine K.M.Duesterhoeft A.Ehrlich S.D.Emmerson P.T.Entian K.-D.Errington J.Fabret C.Ferrari E.Foulger D.Fritz C.Fujita M.Fujita Y.Fuma S.Galizzi A.Galleron N.Ghim S.-Y.Glaser P.Goffeau A.Golightly E.J.Grandi G.Guiseppi G.Guy B.J.Haga K.Haiech J.Harwood C.R.Henaut A.Hilbert H.Holsappel S.Hosono S.Hullo M.-F.Itaya M.Jones L.-M.Joris B.Karamata D.Kasahara Y.Klaerr-Blanchard M.Klein C.Kobayashi Y.Koetter P.Koningstein G.Krogh S.Kumano M.Kurita K.Lapidus A.Lardinois S.Lauber J.Lazarevic V.Lee S.-M.Levine A.Liu H.Masuda S.Mauel C.Medigue C.Medina N.Mellado R.P.Mizuno M.Moestl D.Nakai S.Noback M.Noone D.O'Reilly M.Ogawa K.Ogiwara A.Oudega B.Park S.-H.Parro V.Pohl T.M.Portetelle D.Porwollik S.Prescott A.M.Presecan E.Pujic P.Purnelle B.Rapoport G.Rey M.Reynolds S.Rieger M.Rivolta C.Rocha E.Roche B.Rose M.Sadaie Y.Sato T.Scanlan E.Schleich S.Schroeter R.Scoffone F.Sekiguchi J.Sekowska A.Seror S.J.Serror P.Shin B.-S.Soldo B.Sorokin A.Tacconi E.Takagi T.Takahashi H.Takemaru K.Takeuchi M.Tamakoshi A.Tanaka T.Terpstra P.Tognoni A.Tosato V.Uchiyama S.Vandenbol M.Vannier F.Vassarotti A.Viari A.Wambutt R.Wedler E.Wedler H.Weitzenegger T.Winters P.Wipat A.Yamamoto H.Yamane K.Yasumoto K.Yata K.Yoshida K.Yoshikawa H.-F.Zumstein E.Yoshikawa H.Danchin A.doi:10.1038/367861997Nature390249-256NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Transcriptional regulation of the Bacillus subtilis bscR-CYP102A3 operon by the BscR repressor and differential induction of cytochrome CYP102A3 expression by oleic acid and palmitate.Lee T.-R.Hsu H.-P.Shaw G.-C.doi:10.1093/oxfordjournals.jbchem.a0030202001J. Biochem.130569-574INDUCTIONFatty-acid-displaced transcriptional repressor, a conserved regulator of cytochrome P450 102 transcription in Bacillus species.Gustafsson M.C.Palmer C.N.Wolf C.R.von Wachenfeldt C.doi:10.1007/s0020301003502001Arch. Microbiol.176459-464INDUCTION168 / 1A1Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.Gustafsson M.C.Roitel O.Marshall K.R.Noble M.A.Chapman S.K.Pessegueiro A.Fulco A.J.Cheesman M.R.von Wachenfeldt C.Munro A.W.doi:10.1021/bi035904m2004Biochemistry435474-5487FUNCTIONCATALYTIC ACTIVITYCOFACTORSUBSTRATE SPECIFICITYBIOPHYSICOCHEMICAL PROPERTIESSubstrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis.Lentz O.Urlacher V.Schmid R.D.doi:10.1016/j.jbiotec.2003.11.0012004J. Biotechnol.10841-49FUNCTIONCATALYTIC ACTIVITYSUBSTRATE SPECIFICITYMUTAGENESIS OF PHE-89 AND SER-190168 / ATCC 33234 / DSM 402 / NBRC 111470 / NCIMB 10106Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system.Lentz O.Feenstra A.Habicher T.Hauer B.Schmid R.D.Urlacher V.B.doi:10.1002/cbic.2005002662006ChemBioChem7345-350PROTEIN ENGINEERINGSigM-responsive genes of Bacillus subtilis and their promoters.Jervis A.J.Thackray P.D.Houston C.W.Horsburgh M.J.Moir A.doi:10.1128/jb.00130-072007J. Bacteriol.1894534-4538INDUCTION168 / 1604BacteriaBacteriabifunctional_CYPORCYP120A1Cytochrome P450Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) moduleTranslation factorsBifunctional_P450_P450_redCysJ-like_FAD-bindingCyt_P450Cyt_P450_CSCyt_P450_sfFAD-bd_FR_typeFlavdoxin-likeFlavodoxin/NO_synthFlavoprot_Pyr_Nucl_cyt_RdtaseFlavoprotein-like_sfFNR_nucleotide-bdNADPH_Cyt_P450_Rdtase_alphaOxRdtase_FAD/NAD-bdRiboflavin_synthase-like_b-brlNADPH--CYTOCHROME P450 REDUCTASENITRIC OXIDE SYNTHASE-RELATEDFAD_binding_1Flavodoxin_1NAD_binding_1p450Bifunctional_P450_P450RFLAVODOXINFPNCRCytochrome P450Ferredoxin reductase-like, C-terminal NADP-linked domainFlavoproteinsRiboflavin synthase domain-likeCYTOCHROME_P450FAD_FRFLAVODOXIN_LIKEBifunctional cytochrome P450/NADPH--P450 reductase 2CYP102A3Fatty acid hydroxylase CypBFlavocytochrome P450 102A3Cytochrome P450 102A31.14.14.1NADPH--cytochrome P450 reductase1.6.2.4cypBcyp102A3yrhJBSU27160Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytanic acid hydroxylation. kcat is 3845 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 1690 min(-1) for arachidonic acid hydroxylation. kcat is 3520 min(-1) for the reduction of cytochrome c. kcat is 37050 min(-1) for the reduction of ferricyanide.165 uM for lauric acid542 uM for myristic acid337 uM for palmitic acid68.5 uM for stearic acid28.7 uM for phytanic acid68.3 uM for 15-methylpalmitic acid79 uM for arachidonic acid5.1 uM for NADPH2.43 mM for NADH10.9 uM for cytochrome c (in the reductase assay)285 uM for ferricyanide (in the reductase assay)Negatively regulated by the transcriptional repressor FatR (PubMed:11574077, PubMed:11734890). Is induced by fatty acids such as oleate, linoleate and phytanate, that bind and displace the FatR repressor (PubMed:11734890). Is also induced by palmitate, likely via another mechanism (PubMed:11574077). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).In the N-terminal section; belongs to the cytochrome P450 family.Bifunctional cytochrome P450/NADPH--P450 reductase 211867611054Flavodoxin-like486625FAD-binding FR-type663896Cytochrome P450475Disordered462482NADPH--P450 reductase4761053Basic and acidic residues481axial binding residue403492497539542573575581583Important for catalytic activity271Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with Q-190.V89Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with V-89.Q1901997-07-011118676f4523ae173d36bea5f90aae975f8f3fbMKQASAIPQPKTYGPLKNLPHLEKEQLSQSLWRIADELGPIFRFDFPGVSSVFVSGHNLVAEVCDEKRFDKNLGKGLQKVREFGGDGLFTSWTHEPNWQKAHRILLPSFSQKAMKGYHSMMLDIATQLIQKWSRLNPNEEIDVADDMTRLTLDTIGLCGFNYRFNSFYRDSQHPFITSMLRALKEAMNQSKRLGLQDKMMVKTKLQFQKDIEVMNSLVDRMIAERKANPDENIKDLLSLMLYAKDPVTGETLDDENIRYQIITFLIAGHETTSGLLSFAIYCLLTHPEKLKKAQEEADRVLTDDTPEYKQIQQLKYIRMVLNETLRLYPTAPAFSLYAKEDTVLGGEYPISKGQPVTVLIPKLHRDQNAWGPDAEDFRPERFEDPSSIPHHAYKPFGNGQRACIGMQFALQEATMVLGLVLKHFELINHTGYELKIKEALTIKPDDFKITVKPRKTAAINVQRKEQADIKAETKPKETKPKHGTPLLVLFGSNLGTAEGIAGELAAQGRQMGFTAETAPLDDYIGKLPEEGAVVIVTASYNGAPPDNAAGFVEWLKELEEGQLKGVSYAVFGCGNRSWASTYQRIPRLIDDMMKAKGASRLTAIGEGDAADDFESHRESWENRFWKETMDAFDINEIAQKEDRPSLSITFLSEATETPVAKAYGAFEGIVLENRELQTAASTRSTRHIELEIPAGKTYKEGDHIGILPKNSRELVQRVLSRFGLQSNHVIKVSGSAHMAHLPMDRPIKVVDLLSSYVELQEPASRLQLRELASYTVCPPHQKELEQLVSDDGIYKEQVLAKRLTMLDFLEDYPACEMPFERFLALLPSLKPRYYSISSSPKVHANIVSMTVGVVKASAWSGRGEYRGVASNYLAELNTGDAAACFIRTPQSGFQMPNDPETPMIMVGPGTGIAPFRGFIQARSVLKKEGSTLGEALLYFGCRRPDHDDLYREELDQAEQDGLVTIRRCYSRVENEPKGYVQHLLKQDTQKLMTLIEKGAHIYVCGDGSQMAPDVERTLRLAYEAEKAASQEESAVWLQKLQDQRRYVKDVWTGMtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue