TMLH_NEUCR
ID TMLH_NEUCR Reviewed; 471 AA.
AC Q96UB1; Q7S7S2; Q8NIQ9;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Trimethyllysine dioxygenase;
DE EC=1.14.11.8;
DE AltName: Full=Carnitine biosynthesis protein 1;
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 Name=cbs-1; ORFNames=99H12.050, NCU03802;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12023072; DOI=10.1111/j.1574-6968.2002.tb11154.x;
RA Swiegers J.H., Vaz F.M., Pretorius I.S., Wanders R.J.A., Bauer F.F.;
RT "Carnitine biosynthesis in Neurospora crassa: identification of a cDNA
RT coding for epsilon-N-trimethyllysine hydroxylase and its functional
RT expression in Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 210:19-23(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine
CC (HTML).
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;
CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD11356.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ421151; CAD12887.1; -; mRNA.
DR EMBL; AL451018; CAD11356.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002240; EAA31955.3; -; Genomic_DNA.
DR RefSeq; XP_961191.3; XM_956098.3.
DR AlphaFoldDB; Q96UB1; -.
DR SMR; Q96UB1; -.
DR STRING; 367110.Q96UB1; -.
DR EnsemblFungi; EAA31955; EAA31955; NCU03802.
DR GeneID; 3877351; -.
DR KEGG; ncr:NCU03802; -.
DR VEuPathDB; FungiDB:NCU03802; -.
DR HOGENOM; CLU_021859_2_2_1; -.
DR InParanoid; Q96UB1; -.
DR UniPathway; UPA00118; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050353; F:trimethyllysine dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0045329; P:carnitine biosynthetic process; IBA:GO_Central.
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 Pfam; PF06155; GBBH-like_N; 1.
DR Pfam; PF02668; TauD; 1.
PE 2: Evidence at transcript level;
KW Carnitine biosynthesis; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..471
FT /note="Trimethyllysine dioxygenase"
FT /id="PRO_0000207091"
FT REGION 272..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 174
FT /note="S -> P (in Ref. 1; CAD12887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 52630 MW; EC394240DD720F77 CRC64;
MRPQVVGAIL RSRAVVSRQP LSRTHIFAAV TVAKSSSPAQ NSRRTFSSSF RRLYEPKAEI
TAEGLELSPP QAVTGGKRTV LPNFWLRDNC RCTKCVNQDT LQRNFNTFAI PSDIHPTKVE
ATKENVTVQW SDNHTSTYPW PFLSFYLTSN ARGHENDQIS LWGSEAGSRP PTVSFPRVMA
SDQGVADLTA MIKEFGFCFV KDTPHDDPDV TRQLLERIAF IRVTHYGGFY DFTPDLAMAD
TAYTNLALPA HTDTTYFTDP AGLQAFHLLE HKAAPSRPPP PPPPPPPPSE EKEAAGSAAG
EAAAAAEGGK SLLVDGFNAA RILKEEDPRA YEILSSVRLP WHASGNEGIT IAPDKLYPVL
ELNEDTGELH RVRWNNDDRG VVPFGEKYSP SEWYEAARKW DGILRRKSSE LWVQLEPGKP
LIFDNWRVLH GRSAFSGIRR ICGGYINRDD FISRWRNTNY PRSEVLPRVT G
