[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=1629218 [NCBI, ExPASy, EBI, Israel, Japan] Peterson J.A., Lu J.-Y., Geisselsoder J., Graham-Lorence S., Carmona C., Witney F., Lorence M.C.; "Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon."; J. Biol. Chem. 267:14193-14203(1992).
[2]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). DOI=10.1016/0022-2836(94)90019-1; PubMed=8120894 [NCBI, ExPASy, EBI, Israel, Japan] Hasemann C.A., Ravichandran K.G., Peterson J.A., Deisenhifer J.; "Crystal structure and refinement of cytochrome P450terp at 2.3-A resolution."; J. Mol. Biol. 236:1169-1185(1994).

Comments

FUNCTION: Catalyzes the hydroxylation of alpha-terpineol.
COFACTOR: Heme group.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the cytochrome P450 family.

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

M91440; AAA25996.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A42971; A42971.

3D structure databases

PDB

1CPT; X-ray; 2.30 A; A=1-428.

[ExPASy / RCSB / EBI]

PDBsum

1CPT; -.

ModBase

P33006.

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: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:0004497;	Molecular function: monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002397; Cyt_P450_B.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00359; BP450.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Other

P33006; -.

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

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 428`	`428`	`Cytochrome P450-terp.`	`PRO_0000052222`
`METAL`	`377 377`		`Iron (heme axial ligand).`
`HELIX`	`9 16`	`8`
`HELIX`	`19 22`	`4`
`HELIX`	`24 37`	`14`
`STRAND`	`39 43`	`5`
`STRAND`	`51 54`	`4`
`HELIX`	`57 65`	`9`
`TURN`	`67 69`	`3`
`STRAND`	`70 75`	`6`
`HELIX`	`82 91`	`10`
`TURN`	`92 94`	`3`
`HELIX`	`102 104`	`3`
`HELIX`	`109 118`	`10`
`HELIX`	`123 126`	`4`
`HELIX`	`127 129`	`3`
`HELIX`	`130 145`	`16`
`STRAND`	`147 152`	`6`
`HELIX`	`153 156`	`4`
`TURN`	`157 160`	`4`
`HELIX`	`161 170`	`10`
`HELIX`	`174 176`	`3`
`HELIX`	`177 185`	`9`
`TURN`	`186 188`	`3`
`HELIX`	`208 230`	`23`
`HELIX`	`238 244`	`7`
`STRAND`	`246 251`	`6`
`HELIX`	`254 285`	`32`
`HELIX`	`287 295`	`9`
`HELIX`	`297 299`	`3`
`HELIX`	`300 311`	`12`
`STRAND`	`318 323`	`6`
`STRAND`	`325 327`	`3`
`STRAND`	`330 332`	`3`
`STRAND`	`337 340`	`4`
`HELIX`	`342 345`	`4`
`TURN`	`349 351`	`3`
`HELIX`	`380 394`	`15`
`HELIX`	`395 397`	`3`
`STRAND`	`398 405`	`8`
`STRAND`	`413 415`	`3`
`STRAND`	`417 420`	`4`
`STRAND`	`422 427`	`6`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 47922 Da [This is the MW of the unprocessed precursor]

CRC64: 29B772460CC4E93F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDARATIPEH IARTVILPQG YADDEVIYPA FKWLRDEQPL AMAHIEGYDP MWIATKHADV 

        70         80         90        100        110        120 
MQIGKQPGLF SNAEGSEILY DQNNEAFMRS ISGGCPHVID SLTSMDPPTH TAYRGLTLNW 

       130        140        150        160        170        180 
FQPASIRKLE ENIRRIAQAS VQRLLDFDGE CDFMTDCALY YPLHVVMTAL GVPEDDEPLM 

       190        200        210        220        230        240 
LKLTQDFFGV HEPDEQAVAA PRQSADEAAR RFHETIATFY DYFNGFTVDR RSCPKDDVMS 

       250        260        270        280        290        300 
LLANSKLDGN YIDDKYINAY YVAIATAGHD TTSSSSGGAI IGLSRNPEQL ALAKSDPALI 

       310        320        330        340        350        360 
PRLVDEAVRW TAPVKSFMRT ALADTEVRGQ NIKRGDRIML SYPSANRDEE VFSNPDEFDI 

       370        380        390        400        410        420 
TRFPNRHLGF GWGAHMCLGQ HLAKLEMKIF FEELLPKLKS VELSGPPRLV ATNFVGGPKN 


VPIRFTKA

P33006 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