Reviewed, UniProtKB/Swiss-Prot O08336 (CYPE_BACSU)

Names and origin

Protein names

Recommended name:
    Probable bifunctional P-450/NADPH-P450 reductase 2
Including the following 2 domains:
    1- Recommended name:
            Cytochrome P450 102
              EC=1.14.14.1
    2- Recommended name:
            NADPH--cytochrome P450 reductase
              EC=1.6.2.4

Gene names

Name:	cypE
Synonyms:	CYP102A3, yrhJ
Ordered Locus Names:	BSU27160

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	1054 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Functions as a fatty acid monooxygenase. The reductase domain is required for electron transfer from NADP to cytochrome P450 By similarity.
Catalytic activity	NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein. RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.
Cofactor	FAD By similarity. FMN By similarity. Heme group By similarity.
Subcellular location	Cytoplasm By similarity.
Induction	By palmitate and oleate. Negatively regulated by the transcriptional repressor bscR. Ref.3
Sequence similarities	In the N-terminal section; belongs to the cytochrome P450 family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Ligand	FAD FMN Flavoprotein Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1054	1054	Probable bifunctional P-450/NADPH-P450 reductase 2		PRO_0000052207
Regions
	Domain	486 – 625	140	Flavodoxin-like
	Domain	663 – 896	234	FAD-binding FR-type
	Region	1 – 475	475	Cytochrome P450
	Region	472 – 1053	582	NADPH-P-450 reductase
Sites
	Metal binding	403	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O08336-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 705F8E27866CA110	FASTA	1,054	118,676
	10 20 30 40 50 60 MKQASAIPQP KTYGPLKNLP HLEKEQLSQS LWRIADELGP IFRFDFPGVS SVFVSGHNLV 70 80 90 100 110 120 AEVCDEKRFD KNLGKGLQKV REFGGDGLFT SWTHEPNWQK AHRILLPSFS QKAMKGYHSM 130 140 150 160 170 180 MLDIATQLIQ KWSRLNPNEE IDVADDMTRL TLDTIGLCGF NYRFNSFYRD SQHPFITSML 190 200 210 220 230 240 RALKEAMNQS KRLGLQDKMM VKTKLQFQKD IEVMNSLVDR MIAERKANPD ENIKDLLSLM 250 260 270 280 290 300 LYAKDPVTGE TLDDENIRYQ IITFLIAGHE TTSGLLSFAI YCLLTHPEKL KKAQEEADRV 310 320 330 340 350 360 LTDDTPEYKQ IQQLKYIRMV LNETLRLYPT APAFSLYAKE DTVLGGEYPI SKGQPVTVLI 370 380 390 400 410 420 PKLHRDQNAW GPDAEDFRPE RFEDPSSIPH HAYKPFGNGQ RACIGMQFAL QEATMVLGLV 430 440 450 460 470 480 LKHFELINHT GYELKIKEAL TIKPDDFKIT VKPRKTAAIN VQRKEQADIK AETKPKETKP 490 500 510 520 530 540 KHGTPLLVLF GSNLGTAEGI AGELAAQGRQ MGFTAETAPL DDYIGKLPEE GAVVIVTASY 550 560 570 580 590 600 NGAPPDNAAG FVEWLKELEE GQLKGVSYAV FGCGNRSWAS TYQRIPRLID DMMKAKGASR 610 620 630 640 650 660 LTAIGEGDAA DDFESHRESW ENRFWKETMD AFDINEIAQK EDRPSLSITF LSEATETPVA 670 680 690 700 710 720 KAYGAFEGIV LENRELQTAA STRSTRHIEL EIPAGKTYKE GDHIGILPKN SRELVQRVLS 730 740 750 760 770 780 RFGLQSNHVI KVSGSAHMAH LPMDRPIKVV DLLSSYVELQ EPASRLQLRE LASYTVCPPH 790 800 810 820 830 840 QKELEQLVSD DGIYKEQVLA KRLTMLDFLE DYPACEMPFE RFLALLPSLK PRYYSISSSP 850 860 870 880 890 900 KVHANIVSMT VGVVKASAWS GRGEYRGVAS NYLAELNTGD AAACFIRTPQ SGFQMPNDPE 910 920 930 940 950 960 TPMIMVGPGT GIAPFRGFIQ ARSVLKKEGS TLGEALLYFG CRRPDHDDLY REELDQAEQD 970 980 990 1000 1010 1020 GLVTIRRCYS RVENEPKGYV QHLLKQDTQK LMTLIEKGAH IYVCGDGSQM APDVERTLRL 1030 1040 1050 AYEAEKAASQ EESAVWLQKL QDQRRYVKDV WTGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence 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. Microbiology 143:2939-2943(1997) [PubMed: 9308178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The 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. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"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. J. Biochem. 130:569-574(2001) [PubMed: 11574077] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U93874 Genomic DNA. Translation: AAB80867.1. AL009126 Genomic DNA. Translation: CAB14658.1.
PIR	A69975.
RefSeq	NP_390594.1.
3D structure databases
HSSP	HSSP built from PDB template 1JME based on UniProtKB P14779.
ModBase	Search...
Genome annotation databases
GeneID	937585.
GenomeReviews	Gene locus BSU27160 in contig AL009126_GR.
KEGG	bsu:BSU27160.
NMPDR	fig|224308.1.peg.2719.
Organism-specific databases
SubtiList	BG12299. cypE. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O08336.
OMA	O08336. NEEIDVA.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2712-MON.
BRENDA	1.14.14.1. 150. 1.6.2.4. 150.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR015702. NADPH_Cyt_P450_Rdtase. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19384:SF17. NADPH_Cyt_Red. 1 hit.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYPE_BACSU

Accession

Primary (citable) accession number: O08336

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)