TMLH_CHICK
ID TMLH_CHICK Reviewed; 418 AA.
AC Q5F4B3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Trimethyllysine dioxygenase, mitochondrial;
DE EC=1.14.11.8 {ECO:0000250|UniProtKB:Q9NVH6};
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;
DE Flags: Precursor;
GN Name=TMLHE; ORFNames=RCJMB04_1d18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine
CC (HTML). {ECO:0000250|UniProtKB:Q9NVH6}.
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 Evidence={ECO:0000250|UniProtKB:Q9NVH6};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q91ZW6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9NVH6}.
CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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DR EMBL; AJ851387; CAH65021.1; -; mRNA.
DR RefSeq; NP_001012593.1; NM_001012575.1.
DR RefSeq; XP_015133768.1; XM_015278282.1.
DR RefSeq; XP_015133769.1; XM_015278283.1.
DR RefSeq; XP_015133770.1; XM_015278284.1.
DR AlphaFoldDB; Q5F4B3; -.
DR SMR; Q5F4B3; -.
DR STRING; 9031.ENSGALP00000012029; -.
DR PaxDb; Q5F4B3; -.
DR Ensembl; ENSGALT00000012043; ENSGALP00000012029; ENSGALG00000007443.
DR Ensembl; ENSGALT00000094291; ENSGALP00000072195; ENSGALG00000007443.
DR Ensembl; ENSGALT00000094977; ENSGALP00000066528; ENSGALG00000007443.
DR GeneID; 422296; -.
DR KEGG; gga:422296; -.
DR CTD; 55217; -.
DR VEuPathDB; HostDB:geneid_422296; -.
DR eggNOG; KOG3889; Eukaryota.
DR GeneTree; ENSGT00530000063582; -.
DR HOGENOM; CLU_021859_2_0_1; -.
DR InParanoid; Q5F4B3; -.
DR OMA; EEKVCIQ; -.
DR OrthoDB; 868657at2759; -.
DR PhylomeDB; Q5F4B3; -.
DR TreeFam; TF313805; -.
DR Reactome; R-GGA-71262; Carnitine synthesis.
DR UniPathway; UPA00118; -.
DR PRO; PR:Q5F4B3; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000007443; Expressed in kidney and 12 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050353; F:trimethyllysine dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0045329; P:carnitine biosynthetic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Carnitine biosynthesis; Dioxygenase; Iron; Metal-binding; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..418
FT /note="Trimethyllysine dioxygenase, mitochondrial"
FT /id="PRO_0000260157"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 418 AA; 48656 MW; 01ABB6CF16BD31E5 CRC64;
MWCRRLACLL SVPCQHTRHR LLGPSCGRRT FTAAVARWHH TAPESLSCAW QLHGDHLELR
YADTLMRFDF VWLRDHCRSA SCYNAKTNQR SLDTASVDLS IKPKAVRVDE TTLFLTWPDG
HVTRYGLQWL VKNSYEGQKQ QVMHPRILWN AEIYRQAQVP SVDCQSFLET DEGLKEFLQN
FLLYGIAFVE NVTPTKEDTQ ILAERISLIR ETIYGRMWYF TSDFSRGDTA YTKLALDRHT
DTTYFQEPCG IQVFHCLKHE GTGGRTLLVD GFYAAEQVLR QAPDQFELLS KVPLKHEYIE
NVGDCHNHMI GVGPVLNVYP WNNELYLIRY NNYDRAVINT VPYDVVNRWY TAHRTLTTEL
RRPENELWVK LKPGKALFID NWRVLHGREA FTGYRQLCGC YLTRDDVLNT ARLLGLQA
