ID CYPE_BACSU STANDARD; PRT; 1054 AA. AC O08336; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Probable bifunctional P-450:NADPH-P450 reductase 2 [Includes: DE Cytochrome P450 102 (EC 1.14.14.1); NADPH-cytochrome P450 reductase DE (EC 1.6.2.4)]. GN CYPE OR CYP102A3. OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillus/Clostridium group; OC Bacillus/Staphylococcus group; Bacillus. OX NCBI_TaxID=1423; RN [1] RP SEQUENCE FROM N.A. 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). 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 + 2 FERRICYTOCHROME = NADP(+) + CC 2 FERROCYTOCHROME. CC -!- COFACTOR: BINDS ONE MOLE EACH OF FAD AND FMN (BY SIMILARITY). CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE CYTOCHROME CC P450 FAMILY. 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; -. DR EMBL; Z99117; CAB14658.1; -. DR HSSP; P14779; 1FAG. DR SubtiList; BG12299; cypE. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR003097; FAD_binding. DR InterPro; IPR001709; Flavpyrid_cyt_redctse. DR InterPro; IPR001433; Oxidored_FAD. DR Pfam; PF00667; FAD_binding; 1. DR Pfam; PF00175; oxidored_fad; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00371; FPNCR. DR PRINTS; PR00385; P450. DR PRINTS; PR00464; EP450II. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Electron transport; Membrane; Heme; KW Multifunctional enzyme; FMN; FAD; Flavoprotein; NADP; KW Complete proteome. FT DOMAIN 1 475 CYTOCHROME P450. FT DOMAIN 472 1053 NADPH-P-450 REDUCTASE. FT BINDING 403 403 HEME (BY SIMILARITY). SQ SEQUENCE 1054 AA; 118675 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 //