[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=12023072 [NCBI, ExPASy, EBI, Israel, Japan] Swiegers J.H., Vaz F.M., Pretorius I.S., Wanders R.J.A., Bauer F.F.; "Carnitine biosynthesis in Neurospora crassa: identification of a cDNA coding for epsilon-N-trimethyllysine hydroxylase and its functional expression in Saccharomyces cerevisiae."; FEMS Microbiol. Lett. 210:19-23(2002).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1093/nar/gkg293; PubMed=12655011 [NCBI, ExPASy, EBI, Israel, Japan] Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.; "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."; Nucleic Acids Res. 31:1944-1954(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan] Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; "The genome sequence of the filamentous fungus Neurospora crassa."; Nature 422:859-868(2003).

Comments

FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
CATALYTIC ACTIVITY: N₆,N₆,N⁶-trimethyl-L-lysine + 2-oxoglutarate + O₂ = 3-hydroxy-N₆,N₆,N⁶-trimethyl-L-lysine + succinate + CO₂.
COFACTOR: Iron.
COFACTOR: Ascorbate.
PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the gamma-BBH/TMLD family.
SEQUENCE CAUTION:
- Sequence=CAD11356.1; Type=Erroneous gene model prediction;
- Sequence=EAA31955.2; Type=Erroneous gene model prediction;

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

AJ421151; CAD12887.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL451018; CAD11356.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000011; EAA31955.2; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q96UB1.

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.

Other

ProtoNet

Q96UB1.

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`	`1 471`	`471`	`Trimethyllysine dioxygenase.`	`PRO_0000207091`
`COMPBIAS`	`278 288`	`11`	`Poly-Pro.`
`CONFLICT`	`174 174`		`S -> P (in Ref. 1; CAD12887).`

Sequence information

Length: 471 AA [This is the length of the unprocessed precursor]

Molecular weight: 52630 Da [This is the MW of the unprocessed precursor]

CRC64: EC394240DD720F77 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRPQVVGAIL RSRAVVSRQP LSRTHIFAAV TVAKSSSPAQ NSRRTFSSSF RRLYEPKAEI 

        70         80         90        100        110        120 
TAEGLELSPP QAVTGGKRTV LPNFWLRDNC RCTKCVNQDT LQRNFNTFAI PSDIHPTKVE 

       130        140        150        160        170        180 
ATKENVTVQW SDNHTSTYPW PFLSFYLTSN ARGHENDQIS LWGSEAGSRP PTVSFPRVMA 

       190        200        210        220        230        240 
SDQGVADLTA MIKEFGFCFV KDTPHDDPDV TRQLLERIAF IRVTHYGGFY DFTPDLAMAD 

       250        260        270        280        290        300 
TAYTNLALPA HTDTTYFTDP AGLQAFHLLE HKAAPSRPPP PPPPPPPPSE EKEAAGSAAG 

       310        320        330        340        350        360 
EAAAAAEGGK SLLVDGFNAA RILKEEDPRA YEILSSVRLP WHASGNEGIT IAPDKLYPVL 

       370        380        390        400        410        420 
ELNEDTGELH RVRWNNDDRG VVPFGEKYSP SEWYEAARKW DGILRRKSSE LWVQLEPGKP 

       430        440        450        460        470 
LIFDNWRVLH GRSAFSGIRR ICGGYINRDD FISRWRNTNY PRSEVLPRVT G

Q96UB1 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