ID   TMLH_PICGU              Reviewed;         399 AA.
AC   A5DCB6; Q2V571;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=Trimethyllysine dioxygenase;
DE            EC=1.14.11.8;
DE   AltName: Full=Epsilon-trimethyllysine 2-oxoglutarate dioxygenase;
DE   AltName: Full=TML-alpha-ketoglutarate dioxygenase;
DE            Short=TML dioxygenase;
DE            Short=TMLD;
DE   AltName: Full=TML hydroxylase;
GN   ORFNames=PGUG_00921;
OS   Pichia guilliermondii (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
OX   NCBI_TaxID=4929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Guo C., He P., Lu D., An S., Ning J.;
RT   "Isolation and phylogenetic relationship of aldose reductase in
RT   Candida species.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K.,
RA   Cuomo C., Kellis M., Rasmussen M.D., Grochow J.A., Jaffe D.B.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Zeng Q., Kodira C.D., Yandava C., Alvarado L., O'Leary S.,
RA   Reedy J., Heitman J.;
RT   "The genome sequence of Pichia guilliermondii ATCC 6260.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts trimethyllysine (TML) into
CC       hydroxytrimethyllysine (HTML) (By similarity).
CC   -!- CATALYTIC ACTIVITY: N(6),N(6),N(6)-trimethyl-L-lysine + 2-
CC       oxoglutarate + O(2) = 3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine
CC       + succinate + CO(2).
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- COFACTOR: Ascorbate (By similarity).
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family.
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DR   EMBL; DQ297454; ABB87188.2; -; Genomic_DNA.
DR   EMBL; CH408155; EDK36823.1; -; Genomic_DNA.
DR   RefSeq; XP_001487544.1; -.
DR   GeneID; 5128728; -.
DR   BRENDA; 1.14.11.8; 3704.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0050353; F:trimethyllysine dioxygenase activity; IEA:EC.
DR   GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003819; Taurine_dOase.
DR   InterPro; IPR012776; Trimethyllysine_dOase.
DR   PANTHER; PTHR10696:SF2; tMLys_dOase; 1.
DR   Pfam; PF02668; TauD; 1.
DR   TIGRFAMs; TIGR02410; carnitine_TMLD; 1.
PE   3: Inferred from homology;
KW   Carnitine biosynthesis; Complete proteome; Cytoplasm; Dioxygenase;
KW   Iron; Oxidoreductase.
FT   CHAIN         1    399       Trimethyllysine dioxygenase.
FT                                /FTId=PRO_0000295035.
FT   CONFLICT     27     27       L -> S (in Ref. 1; ABB87188).
FT   CONFLICT    318    318       L -> S (in Ref. 1; ABB87188).
FT   CONFLICT    386    386       N -> K (in Ref. 1; ABB87188).
SQ   SEQUENCE   399 AA;  46319 MW;  0DD2D016195D130F CRC64;
     MTKMDHKIVK TSYDGDAVSV EWDGGALAKF DNIWLRDNCH CSECYYDATK QRLLNSCSIP
     DDIAPIKVDS SPTKLKIVWN HEEHQSEYEC RWLVIHSYNP RQIPVTEKVS GEREILAREY
     WTVKDMEGRL PSVDFKTVMA STDENEEPIK DWCLKIWKHG FCFIDNVPVD PQETEKLCEK
     LMYIRPTHYG GFWDFTSDLS KNDTAYTNID ISSHTDGTYW SDTPGLQLFH LLMHEGTGGT
     TSLVDAFHCA EILKKEHPES FELLTRIPVP AHSAGEEKVC IQPDIPQPIF KLDTNGELIQ
     VRWNQSDRST MDSWENPLEV VKFYRAIKQW HKIISDPANE LFYQLRPGQC LIFDNWRCFH
     SRTEFTGKRR MCGAYINRDD FVSRLNLLNI GRQPVLDAI
//