Reviewed, UniProtKB/Swiss-Prot A5DCB6 (TMLH_PICGU)

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

ORF Names:

PGUG_00921

Organism

Pichia guilliermondii (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

4929 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML) By similarity.
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 By similarity. Ascorbate By similarity.
Pathway	Amine and polyamine biosynthesis; carnitine biosynthesis.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the gamma-BBH/TMLD family.

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 electron carrier activity 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 – 399	399	Trimethyllysine dioxygenase		PRO_0000295035
Experimental info
	Sequence conflict	27	1	L → S in ABB87188. Ref.1
	Sequence conflict	318	1	L → S in ABB87188. Ref.1
	Sequence conflict	386	1	N → K in ABB87188. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A5DCB6-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 0DD2D016195D130F	FASTA	399	46,319
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and phylogenetic relationship of aldose reductase in Candida species." Guo C., He P., Lu D., An S., Ning J. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Pichia guilliermondii ATCC 6260." 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. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ297454 Genomic DNA. Translation: ABB87188.2. CH408155 Genomic DNA. Translation: EDK36823.1.
RefSeq	XP_001487544.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5128728.
Enzyme and pathway databases
BRENDA	1.14.11.8. 3704.
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_PICGU

Accession

Primary (citable) accession number: A5DCB6
Secondary accession number(s): Q2V571

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	June 12, 2007
Last modified:	June 16, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)