ID A0A1Q5T0U8_9EURO Unreviewed; 688 AA.
AC A0A1Q5T0U8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Trimethyllysine dioxygenase {ECO:0000313|EMBL:OKO93889.1};
GN ORFNames=PENSUB_12168 {ECO:0000313|EMBL:OKO93889.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO93889.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO93889.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO93889.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKO93889.1}.
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DR EMBL; MNBE01000723; OKO93889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5T0U8; -.
DR STRING; 1316194.A0A1Q5T0U8; -.
DR OrthoDB; 2140828at2759; -.
DR UniPathway; UPA00118; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0050353; F:trimethyllysine dioxygenase activity; IEA:InterPro.
DR GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00250; CAS_like; 1.
DR CDD; cd03448; HDE_HSD; 1.
DR Gene3D; 3.60.130.10; Clavaminate synthase-like; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR InterPro; IPR012776; Trimethyllysine_dOase.
DR NCBIfam; TIGR02410; carnitine_TMLD; 1.
DR PANTHER; PTHR13078:SF57; DEHYDRATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G00640)-RELATED; 1.
DR PANTHER; PTHR13078; PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 2-RELATED; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF02668; TauD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:OKO93889.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 173..286
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT DOMAIN 408..648
FT /note="TauD/TfdA-like"
FT /evidence="ECO:0000259|Pfam:PF02668"
SQ SEQUENCE 688 AA; 76559 MW; 51E216C19CCCDB44 CRC64;
MSAPGAGHEF PAQEVSWQKR DVLLFANSIG AKADELHFLY ELHPNFAVFP TYPLILPFKL
TDQEVTDFYA RQKAVKIPGV PDLDHRRGVD GQRKITVLKP LPPTSAGRKF QLRNKVIGVY
DKGKPGTVME TEQSIVDAET GEVYSKVVSS GFLVGQGGWG GPKGPATVNF PPPEGKKPDA
VHVVQTNLET AHLYRLNGDY NPLHADPVPG QKMGFGGTII HGLFSWNSAA HGILRELGGS
NAENLKEFQA RFASPVRPGD KLTTEIWRTG DVQADGFEEI RFVTKNQTGK AVLSNGRALV
KVTGAKSKLT DSVQLVIASR NVAPLARSAN LPSNVSKRLL SDSTQPQATF QEINVTNDPF
DEKSTQLAYR SALKSGNVVI KTNSKTGAPF WQLPFKAYDP EKGNPYPEVA YEDVMSKDAA
VLEWLEKIWV WGFCFVKGVP VNPESTKTLI ERIAFIRHTH YGGFWDFTAD LTYKDTAYTN
ELLGAHTDNT YFTDPARLQL FHLLSHTDGT GGESLLVDGF AAAKALSKDS PDFYNSLASS
RHPWHASGND DVCIQPSTTA PVLKVHPDTK AVYQVRWNNY DRAPKTSWHV SEQKDWYMAA
RAYNDILTKP SNEIRTQLQP GTALIFDNWR MLHGRSEFTG KRRMCGGYVN NDDFISRLRL
LKFGRQTVLD NLGNTRGWQN RENPYSIY
//
