ID   CYPD_BACSU              Reviewed;        1061 AA.
AC   O08394;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 85.
DE   RecName: Full=Probable bifunctional P-450/NADPH-P450 reductase 1;
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=cypD; Synonyms=CYP102A2, yetO, yfnJ; OrderedLocusNames=BSU07250;
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).
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   -!- 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.
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DR   EMBL; D87979; BAA20123.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12544.1; -; Genomic_DNA.
DR   PIR; D69799; D69799.
DR   RefSeq; NP_388606.1; -.
DR   HSSP; P14779; 1JPZ.
DR   GeneID; 938784; -.
DR   GenomeReviews; AL009126_GR; BSU07250.
DR   KEGG; bsu:BSU07250; -.
DR   NMPDR; fig|224308.1.peg.725; -.
DR   SubtiList; BG12871; cypD.
DR   HOGENOM; O08394; -.
DR   OMA; O08394; EASHASI.
DR   BioCyc; BSUB224308:BSU0725-MON; -.
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; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR015702; NADPH_Cyt_P450_Rdtase.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 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   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Electron transport; FAD; Flavoprotein;
KW   FMN; Heme; Iron; Metal-binding; Monooxygenase; Multifunctional enzyme;
KW   NADP; Oxidoreductase; Transport.
FT   CHAIN         1   1061       Probable bifunctional P-450/NADPH-P450
FT                                reductase 1.
FT                                /FTId=PRO_0000052206.
FT   DOMAIN      493    632       Flavodoxin-like.
FT   DOMAIN      671    904       FAD-binding FR-type.
FT   REGION        1    474       Cytochrome P450.
FT   REGION      475   1061       NADPH-P-450 reductase.
FT   METAL       403    403       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   1061 AA;  119468 MW;  7915DACC20578978 CRC64;
     MKETSPIPQP KTFGPLGNLP LIDKDKPTLS LIKLAEEQGP IFQIHTPAGT TIVVSGHELV
     KEVCDEERFD KSIEGALEKV RAFSGDGLFT SWTHEPNWRK AHNILMPTFS QRAMKDYHEK
     MVDIAVQLIQ KWARLNPNEA VDVPGDMTRL TLDTIGLCGF NYRFNSYYRE TPHPFINSMV
     RALDEAMHQM QRLDVQDKLM VRTKRQFRYD IQTMFSLVDS IIAERRANGD QDEKDLLARM
     LNVEDPETGE KLDDENIRFQ IITFLIAGHE TTSGLLSFAT YFLLKHPDKL KKAYEEVDRV
     LTDAAPTYKQ VLELTYIRMI LNESLRLWPT APAFSLYPKE DTVIGGKFPI TTNDRISVLI
     PQLHRDRDAW GKDAEEFRPE RFEHQDQVPH HAYKPFGNGQ RACIGMQFAL HEATLVLGMI
     LKYFTLIDHE NYELDIKQTL TLKPGDFHIS VQSRHQEAIH ADVQAAEKAA PDEQKEKTEA
     KGASVIGLNN RPLLVLYGSD TGTAEGVARE LADTASLHGV RTKTAPLNDR IGKLPKEGAV
     VIVTSSYNGK PPSNAGQFVQ WLQEIKPGEL EGVHYAVFGC GDHNWASTYQ YVPRFIDEQL
     AEKGATRFSA RGEGDVSGDF EGQLDEWKKS MWADAIKAFG LELNENADKE RSTLSLQFVR
     GLGESPLARS YEASHASIAE NRELQSADSD RSTRHIEIAL PPDVEYQEGD HLGVLPKNSQ
     TNVSRILHRF GLKGTDQVTL SASGRSAGHL PLGRPVSLHD LLSYSVEVQE AATRAQIREL
     ASFTVCPPHR RELEELSAEG VYQEQILKKR ISMLDLLEKY EACDMPFERF LELLRPLKPR
     YYSISSSPRV NPRQASITVG VVRGPAWSGR GEYRGVASND LAERQAGDDV VMFIRTPESR
     FQLPKDPETP IIMVGPGTGV APFRGFLQAR DVLKREGKTL GEAHLYFGCR NDRDFIYRDE
     LERFEKDGIV TVHTAFSRKE GMPKTYVQHL MADQADTLIS ILDRGGRLYV CGDGSKMAPD
     VEAALQKAYQ AVHGTGEQEA QNWLRHLQDT GMYAKDVWAG I
//