NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Guo C., He P., Lu D., An S., Ning J.;
"Isolation and phylogenetic relationship of aldose reductase in Candida species.";
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324;
Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C., Kellis M., Rasmussen M.D., Grochow J.A., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K., LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., Zeng Q., Kodira C.D., Yandava C., Alvarado L., O'Leary S., Reedy J., Heitman J.;
"The genome sequence of Pichia guilliermondii ATCC 6260.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML) (By similarity).
CATALYTIC ACTIVITY: N₆,N₆,N⁶-trimethyl-L-lysine + 2-oxoglutarate + O₂ = 3-hydroxy-N₆,N₆,N⁶-trimethyl-L-lysine + succinate + CO₂.
COFACTOR: Iron (By similarity).
COFACTOR: Ascorbate (By similarity).
PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the gamma-BBH/TMLD 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

DQ297454; ABB87188.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH408155; EDK36823.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001487544.1; -.

3D structure databases

ModBase

A5DCB6.

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: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 InterPro).
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:0050353;	Molecular function: trimethyllysine dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0045329;	Biological process: carnitine biosynthetic process (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

IPR003819; Taurine_dOase.
IPR012776; Trimethyllysine_dOase.
Graphical view of domain structure.

PANTHER

PTHR10696:SF2; tMLys_dOase; 1.

Pfam

PF02668; TauD; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02410; carnitine_TMLD; 1.

Genome annotation databases

GeneID

5128728; -.

Other

ProtoNet

A5DCB6.

UniRef

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

Keywords

Carnitine biosynthesis; Complete proteome; Cytoplasm; Dioxygenase; Iron; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 399`	`399`	`Trimethyllysine dioxygenase.`	`PRO_0000295035`
`CONFLICT`	`27 27`		`L -> S (in Ref. 1; ABB87188).`
`CONFLICT`	`318 318`		`L -> S (in Ref. 1; ABB87188).`
`CONFLICT`	`386 386`		`N -> K (in Ref. 1; ABB87188).`

Sequence information

Length: 399 AA [This is the length of the unprocessed precursor]

Molecular weight: 46319 Da [This is the MW of the unprocessed precursor]

CRC64: 0DD2D016195D130F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKMDHKIVK TSYDGDAVSV EWDGGALAKF DNIWLRDNCH CSECYYDATK QRLLNSCSIP 

        70         80         90        100        110        120 
DDIAPIKVDS SPTKLKIVWN HEEHQSEYEC RWLVIHSYNP RQIPVTEKVS GEREILAREY 

       130        140        150        160        170        180 
WTVKDMEGRL PSVDFKTVMA STDENEEPIK DWCLKIWKHG FCFIDNVPVD PQETEKLCEK 

       190        200        210        220        230        240 
LMYIRPTHYG GFWDFTSDLS KNDTAYTNID ISSHTDGTYW SDTPGLQLFH LLMHEGTGGT 

       250        260        270        280        290        300 
TSLVDAFHCA EILKKEHPES FELLTRIPVP AHSAGEEKVC IQPDIPQPIF KLDTNGELIQ 

       310        320        330        340        350        360 
VRWNQSDRST MDSWENPLEV VKFYRAIKQW HKIISDPANE LFYQLRPGQC LIFDNWRCFH 

       370        380        390 
SRTEFTGKRR MCGAYINRDD FVSRLNLLNI GRQPVLDAI

A5DCB6 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