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Database: UniProt
Entry: Q4S1W4_TETNG
LinkDB: Q4S1W4_TETNG
Original site: Q4S1W4_TETNG 
ID   Q4S1W4_TETNG            Unreviewed;      1005 AA.
AC   Q4S1W4;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=2-oxoadipate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040865};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=2-oxoadipate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041619};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
DE   AltName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE   AltName: Full=Alpha-ketoadipate dehydrogenase {ECO:0000256|ARBA:ARBA00042817};
DE   AltName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042094};
DE   AltName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial {ECO:0000256|ARBA:ARBA00042537};
DE   Flags: Fragment;
GN   ORFNames=GSTENG00025361001 {ECO:0000313|EMBL:CAG05368.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG05368.1};
RN   [1] {ECO:0000313|EMBL:CAG05368.1, ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAG05368.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSTNIP00000016566.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoadipate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-glutaryldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:69576, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:17726, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57499, ChEBI:CHEBI:83099, ChEBI:CHEBI:184385;
CC         Evidence={ECO:0000256|ARBA:ARBA00036608};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC         Evidence={ECO:0000256|ARBA:ARBA00036608};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00033699};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC         Evidence={ECO:0000256|ARBA:ARBA00033699};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   EMBL; CAAE01014764; CAG05368.1; -; Genomic_DNA.
DR   STRING; 99883.ENSTNIP00000016566; -.
DR   Ensembl; ENSTNIT00000016780.1; ENSTNIP00000016566.1; ENSTNIG00000013569.1.
DR   KEGG; tng:GSTEN00025361G001; -.
DR   GeneTree; ENSGT00950000183125; -.
DR   HOGENOM; CLU_004709_1_1_1; -.
DR   OMA; ATEWRNT; -.
DR   TreeFam; TF300695; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 2.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 2.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 2.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 3.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          623..869
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          981..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1005
FT                   /evidence="ECO:0000313|EMBL:CAG05368.1"
SQ   SEQUENCE   1005 AA;  113926 MW;  1683DC40E1EB15FB CRC64;
     MHHLRTTFLR LRPLTAAQAA QRLSQPRLSA MAEGSRTFQP SRQLNTSEPF LNGTSSNYIE
     EMYLAWLENP KSVHKSWEVY FRNVNAGVPP GAAYQSPSSL GEPPQGLRTL VGIQPNIEEL
     VTDHLAVYSL IRAYQGCTIH WVEEGSYGLN ESHMDKVFWL PKTTYIGGSE SALPLREIIH
     RLETAYCQHI GVEFMFINNL EQCQWIRQRF ETPGLMKLSL EEKRTLLNRV IKSTRFEEFL
     HKKWSSEKRF GLEGCESLIP ALKTIIDESS KSGVESVIMG MPHRGRLNVL ANVFHKELDQ
     ILCQFDPKLE AADEGSGDVK YHLGTYQKRF NPVSKKDIMM SLMANPSHLE AVDPVVQGKT
     KAEQFYCDDT EGKKVMSLLL HGDAAFAGQG VVYETFHLSD LPSYTTHGTI HVVVNNQIGF
     TTDPRVARSS PHPTDVARVV NAPIFHVNAD DAEAVIYVCK VATEWRNTFH KDVVVDLVCY
     RRNGHNEMDE PMFTQPLMYK KIRKQKGVLT KCAEKFISDG VITQQEYKEK VAQYDKICED
     AHNRSKDMKV LENKHWLSSP WPEFFKLDGE PKTMSCDSTG IPEEQLRHIG NVASSVPLEK
     LTIHGGLTRI LKARADMVNK RVCDWALGEY MAFGSLLQDG IHVRLSGQDV ERGTFSHRHH
     VLHDQNIDKE NYIPLNHISH GQARYTVCNS SLSEYGVLGF ELGFAMASPN ALVLWEAQFG
     DFHNTAQCII DQFISSGQAK WVRQSGIVLL LPHGMEGMVK HKTPSTPFRL TSSQPVNMSL
     LPFCPIFCPS QGPEHSSARP ERFLQMCNDD PDVFPEVTED FAVRQLCDCN WIVVNCSTPA
     SYFHALRRQI LLPFRKPLIV FTPKSLLRQA RSSFDDMLPG THFRRIIPDD GPASVHPQEV
     KRVIFCTGKI YYKLIQEREG RGLDDTVAVV RLEQLSPFPF DLVKAEIDQY TNAELVWCQE
     EHKNQGYYNY IKPRLSASSG HTRPVRYAGR EPAAAPATGN KRTHE
//
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