NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9308178 [NCBI, ExPASy, EBI, Israel, Japan]
Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J., Duesterhoeft A., Ehrlich S.D.;
"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.";
Microbiology 143:2939-2943(1997).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).

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.
CATALYTIC ACTIVITY: RH + reduced flavoprotein + O₂ = ROH + oxidized flavoprotein + H₂O.
COFACTOR: FAD (By similarity).
COFACTOR: FMN (By similarity).
COFACTOR: Heme group (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: In the N-terminal section; belongs to the cytochrome P450 family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D87979; BAA20123.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99107; CAB12544.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D69799; D69799.

RefSeq

NP_388606.1; -.

3D structure databases

HSSP

P14779; 1JPZ. [HSSP ENTRY / PDB]

ModBase

O08394.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU0725-MON; -.

Organism-specific databases

SubtiList

BG12871; cypD. [Micado]

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0003958;	Molecular function: NADPH-hemoprotein reductase activity (inferred from electronic annotation from EC).
GO:0050381;	Molecular function: unspecific monooxygenase activity (inferred from electronic annotation from EC).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19384:SF17; NADPH_Cyt_Red; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00369; FLAVODOXIN.
PR00371; FPNCR.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.
PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

O08394.

Genome annotation databases

GeneID

938784; -.

GenomeReviews

AL009126_GR; BSU07250.

KEGG

bsu:BSU07250; -.

NMPDR

fig|224308.1.peg.725; -.

Phylogenomic databases

HOGENOM

O08394; -.

Genome annotation databases

CMR

O08394; BSU07250.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Electron transport; FAD; Flavoprotein; FMN; Heme; Iron; Metal-binding; Monooxygenase; Multifunctional enzyme; NADP; Oxidoreductase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1061`	`1061`	`Probable bifunctional P-450/NADPH-P450 reductase 1.`	`PRO_0000052206`
`DOMAIN`	`493 632`	`140`	`Flavodoxin-like.`
`DOMAIN`	`671 904`	`234`	`FAD-binding FR-type.`
`REGION`	`1 474`	`474`	`Cytochrome P450.`
`REGION`	`475 1061`	`587`	`NADPH-P-450 reductase.`
`METAL`	`403 403`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 1061 AA [This is the length of the unprocessed precursor]

Molecular weight: 119468 Da [This is the MW of the unprocessed precursor]

CRC64: 7915DACC20578978 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKETSPIPQP KTFGPLGNLP LIDKDKPTLS LIKLAEEQGP IFQIHTPAGT TIVVSGHELV 

        70         80         90        100        110        120 
KEVCDEERFD KSIEGALEKV RAFSGDGLFT SWTHEPNWRK AHNILMPTFS QRAMKDYHEK 

       130        140        150        160        170        180 
MVDIAVQLIQ KWARLNPNEA VDVPGDMTRL TLDTIGLCGF NYRFNSYYRE TPHPFINSMV 

       190        200        210        220        230        240 
RALDEAMHQM QRLDVQDKLM VRTKRQFRYD IQTMFSLVDS IIAERRANGD QDEKDLLARM 

       250        260        270        280        290        300 
LNVEDPETGE KLDDENIRFQ IITFLIAGHE TTSGLLSFAT YFLLKHPDKL KKAYEEVDRV 

       310        320        330        340        350        360 
LTDAAPTYKQ VLELTYIRMI LNESLRLWPT APAFSLYPKE DTVIGGKFPI TTNDRISVLI 

       370        380        390        400        410        420 
PQLHRDRDAW GKDAEEFRPE RFEHQDQVPH HAYKPFGNGQ RACIGMQFAL HEATLVLGMI 

       430        440        450        460        470        480 
LKYFTLIDHE NYELDIKQTL TLKPGDFHIS VQSRHQEAIH ADVQAAEKAA PDEQKEKTEA 

       490        500        510        520        530        540 
KGASVIGLNN RPLLVLYGSD TGTAEGVARE LADTASLHGV RTKTAPLNDR IGKLPKEGAV 

       550        560        570        580        590        600 
VIVTSSYNGK PPSNAGQFVQ WLQEIKPGEL EGVHYAVFGC GDHNWASTYQ YVPRFIDEQL 

       610        620        630        640        650        660 
AEKGATRFSA RGEGDVSGDF EGQLDEWKKS MWADAIKAFG LELNENADKE RSTLSLQFVR 

       670        680        690        700        710        720 
GLGESPLARS YEASHASIAE NRELQSADSD RSTRHIEIAL PPDVEYQEGD HLGVLPKNSQ 

       730        740        750        760        770        780 
TNVSRILHRF GLKGTDQVTL SASGRSAGHL PLGRPVSLHD LLSYSVEVQE AATRAQIREL 

       790        800        810        820        830        840 
ASFTVCPPHR RELEELSAEG VYQEQILKKR ISMLDLLEKY EACDMPFERF LELLRPLKPR 

       850        860        870        880        890        900 
YYSISSSPRV NPRQASITVG VVRGPAWSGR GEYRGVASND LAERQAGDDV VMFIRTPESR 

       910        920        930        940        950        960 
FQLPKDPETP IIMVGPGTGV APFRGFLQAR DVLKREGKTL GEAHLYFGCR NDRDFIYRDE 

       970        980        990       1000       1010       1020 
LERFEKDGIV TVHTAFSRKE GMPKTYVQHL MADQADTLIS ILDRGGRLYV CGDGSKMAPD 

      1030       1040       1050       1060 
VEAALQKAYQ AVHGTGEQEA QNWLRHLQDT GMYAKDVWAG I

O08394 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools