Reviewed, UniProtKB/Swiss-Prot Q96UB1 (TMLH_NEUCR)

Names and origin

Protein names

Recommended name:
    Trimethyllysine dioxygenase
    EC=1.14.11.8
Alternative name(s):
    Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
    TML-alpha-ketoglutarate dioxygenase
      Short name=TML dioxygenase
      Short name=TMLD
    TML hydroxylase

Gene names

Name:	cbs-1
ORF Names:	99H12.050, NCU03802

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
Catalytic activity	N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2.
Cofactor	Iron. Ascorbate.
Pathway	Amine and polyamine biosynthesis; carnitine biosynthesis.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the gamma-BBH/TMLD family.
Sequence caution	The sequence CAD11356.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA31955.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carnitine biosynthesis
Cellular component	Cytoplasm
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carnitine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW trimethyllysine dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 471	471	Trimethyllysine dioxygenase		PRO_0000207091
Regions
	Compositional bias	278 – 288	11	Poly-Pro
Sites
	Binding site	251	1	2-oxoglutarate Probable
	Binding site	253	1	2-oxoglutarate Probable
	Binding site	430	1	2-oxoglutarate Probable
Experimental info
	Sequence conflict	174	1	S → P in CAD12887. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q96UB1-1 [UniParc]. Last modified June 20, 2002. Version 2. Checksum: EC394240DD720F77	FASTA	471	52,630
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Carnitine biosynthesis in Neurospora crassa: identification of a cDNA coding for epsilon-N-trimethyllysine hydroxylase and its functional expression in Saccharomyces cerevisiae." Swiegers J.H., Vaz F.M., Pretorius I.S., Wanders R.J.A., Bauer F.F. FEMS Microbiol. Lett. 210:19-23(2002) [PubMed: 12023072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"The genome sequence of the filamentous fungus Neurospora crassa." 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. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ421151 mRNA. Translation: CAD12887.1. AL451018 Genomic DNA. Translation: CAD11356.1. Sequence problems. AABX02000011 Genomic DNA. Translation: EAA31955.2. Sequence problems.
3D structure databases
SMR	Q96UB1. Positions 171-443.
ModBase	Search...
Phylogenomic databases
eggNOG	fuNOG07855.
OrthoDB	EOG91NW3J.
Enzyme and pathway databases
BRENDA	1.14.11.8. 266.
Family and domain databases
InterPro	IPR003819. Taurine_dOase. IPR012776. Trimethyllysine_dOase. [Graphical view]
PANTHER	PTHR10696:SF2. tMLys_dOase. 1 hit.
Pfam	PF02668. TauD. 1 hit. [Graphical view]
TIGRFAMs	TIGR02410. carnitine_TMLD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TMLH_NEUCR

Accession

Primary (citable) accession number: Q96UB1
Secondary accession number(s): Q7S7S2, Q8NIQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	June 20, 2002
Last modified:	February 9, 2010
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)