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   16-JUN-2009, entry version 47.
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   Name=cbs-1; ORFNames=99H12.050, NCU03802;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22017891; PubMed=12023072;
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   MEDLINE=22542210; PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora 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   MEDLINE=22598136; 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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   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.,
RA   Paulsen I., 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
CC       hydroxytrimethyllysine (HTML).
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.
CC   -!- COFACTOR: Ascorbate.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD11356.1; Type=Erroneous gene model prediction;
CC       Sequence=EAA31955.2; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ421151; CAD12887.1; -; mRNA.
DR   EMBL; AL451018; CAD11356.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AABX02000011; EAA31955.2; ALT_SEQ; Genomic_DNA.
DR   BRENDA; 1.14.11.8; 266.
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   2: Evidence at transcript level;
KW   Carnitine biosynthesis; Complete proteome; Cytoplasm; Dioxygenase;
KW   Iron; Oxidoreductase.
FT   CHAIN         1    471       Trimethyllysine dioxygenase.
FT                                /FTId=PRO_0000207091.
FT   COMPBIAS    278    288       Poly-Pro.
FT   CONFLICT    174    174       S -> P (in Ref. 1; CAD12887).
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
//