[1]	NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE. TISSUE=Root; PubMed=2033047 [NCBI, ExPASy, EBI, Israel, Japan] Matsuda J., Okabe S., Hashimoto T., Yamada Y.; "Molecular cloning of hyoscyamine 6 beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, from cultured roots of Hyoscyamus niger."; J. Biol. Chem. 266:9460-9464(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1104/pp.105.2.483; PubMed=8066129 [NCBI, ExPASy, EBI, Israel, Japan] Kanegae T., Kajiya H., Amano Y., Hashimoto T., Yamada Y.; "Species-dependent expression of the hyoscyamine 6 beta-hydroxylase gene in the pericycle."; Plant Physiol. 105:483-490(1994).

Comments

CATALYTIC ACTIVITY: L-hyoscyamine + 2-oxoglutarate + O₂ = (6S)-hydroxyhyoscyamine + succinate + CO₂.
COFACTOR: Iron.
COFACTOR: Ascorbate.
PATHWAY: Alkaloid biosynthesis; scopolamine biosynthesis .
SUBUNIT: Monomer.
TISSUE SPECIFICITY: Root.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase 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

M62719; AAA33387.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D26583; BAA05630.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40005; A40005.

3D structure databases

ModBase

P24397.

Ontologies

GO:0047998;	Molecular function: hyoscyamine (6S)-dioxygenase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
IPR002283; Isopenicillin-N_synthase.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

PRINTS

PR00682; IPNSYNTHASE.

ProtoNet

P24397.

Other

UniRef

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

Keywords

Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase; Vitamin C.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 344`	`344`	`Hyoscyamine 6-dioxygenase.`	`PRO_0000067281`
`METAL`	`217 217`		`Iron (Potential).`
`METAL`	`274 274`		`Iron (Potential).`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 39001 Da [This is the MW of the unprocessed precursor]

CRC64: 2618501AC1587F24 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATFVSNWST KSVSESFIAP LQKRAEKDVP VGNDVPIIDL QQHHHLLVQQ ITKACQDFGL 

        70         80         90        100        110        120 
FQVINHGFPE ELMLETMEVC KEFFALPAEE KEKFKPKGEA AKFELPLEQK AKLYVEGEQL 

       130        140        150        160        170        180 
SNEEFLYWKD TLAHGCHPLD QDLVNSWPEK PAKYREVVAK YSVEVRKLTM RMLDYICEGL 

       190        200        210        220        230        240 
GLKLGYFDNE LSQIQMMLTN YYPPCPDPSS TLGSGGHYDG NLITLLQQDL PGLQQLIVKD 

       250        260        270        280        290        300 
ATWIAVQPIP TAFVVNLGLT LKVITNEKFE GSIHRVVTDP TRDRVSIATL IGPDYSCTIE 

       310        320        330        340 
PAKELLNQDN PPLYKPYSYS EFADIYLSDK SDYDSGVKPY KINV

P24397 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