TMLH_PICGU
ID TMLH_PICGU Reviewed; 399 AA.
AC A5DCB6; Q2V571;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Trimethyllysine dioxygenase;
DE EC=1.14.11.8;
DE AltName: Full=Epsilon-trimethyllysine 2-oxoglutarate dioxygenase;
DE AltName: Full=TML hydroxylase;
DE AltName: Full=TML-alpha-ketoglutarate dioxygenase;
DE Short=TML dioxygenase;
DE Short=TMLD;
GN ORFNames=PGUG_00921;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
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 Candida
RT 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 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine
CC (HTML). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 =
CC (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate;
CC Xref=Rhea:RHEA:14181, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58100,
CC ChEBI:CHEBI:141499; EC=1.14.11.8;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ297454; ABB87188.2; -; Genomic_DNA.
DR EMBL; CH408155; EDK36823.2; -; Genomic_DNA.
DR RefSeq; XP_001487544.1; XM_001487494.1.
DR AlphaFoldDB; A5DCB6; -.
DR SMR; A5DCB6; -.
DR STRING; 4929.XP_001487544.1; -.
DR EnsemblFungi; EDK36823; EDK36823; PGUG_00921.
DR GeneID; 5128728; -.
DR KEGG; pgu:PGUG_00921; -.
DR eggNOG; KOG3889; Eukaryota.
DR HOGENOM; CLU_021859_2_2_1; -.
DR InParanoid; A5DCB6; -.
DR OMA; EEKVCIQ; -.
DR OrthoDB; 868657at2759; -.
DR UniPathway; UPA00118; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050353; F:trimethyllysine dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.2020.30; -; 1.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR010376; GBBH-like_N.
DR InterPro; IPR038492; GBBH-like_N_sf.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR InterPro; IPR012776; Trimethyllysine_dOase.
DR Pfam; PF06155; GBBH-like_N; 1.
DR Pfam; PF02668; TauD; 1.
DR TIGRFAMs; TIGR02410; carnitine_TMLD; 1.
PE 3: Inferred from homology;
KW Carnitine biosynthesis; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..399
FT /note="Trimethyllysine dioxygenase"
FT /id="PRO_0000295035"
FT BINDING 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 386
FT /note="N -> K (in Ref. 1; ABB87188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 46267 MW; 5A67A099DD08D604 CRC64;
MTKMDHKIVK TSYDGDAVSV EWDGGASAKF 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 MDSWENPSEV VKFYRAIKQW HKIISDPANE LFYQLRPGQC LIFDNWRCFH
SRTEFTGKRR MCGAYINRDD FVSRLNLLNI GRQPVLDAI
