ID G3NKN9_GASAC Unreviewed; 898 AA.
AC G3NKN9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=2-oxoadipate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040865};
DE AltName: Full=2-oxoadipate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041619};
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};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000005902.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000005902.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000005902.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:ARBA00043772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC Evidence={ECO:0000256|ARBA:ARBA00043772};
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 AlphaFoldDB; G3NKN9; -.
DR Ensembl; ENSGACT00000005919.1; ENSGACP00000005902.1; ENSGACG00000004439.1.
DR GeneTree; ENSGT00950000183125; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000004439; Expressed in muscle tissue and 11 other cell types or tissues.
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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
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; 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 NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 549..752
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 100150 MW; 2A394781A626FDE7 CRC64;
YHTEKGVFGY RPKEPERHRH KSQSDRIAAL NQDHRLARLV EAYRAHGHKA AKINPLQPEQ
PVAASVPEIN MLTGTMTGRL QTAGLQHFGR AEASVEEVQA YLEGAYCGSL SVETSQLSSL
EEREWFSDRF EELKKASFSA EERKQLAKVM LESQEFDHFL ATKFSTVKRY GGEGAESMMG
FFYELFHHSS HSGVTDIIIG MPHRGRLNLL TGLLKFPPEL MFRKMRGLSE FPDTSPATGD
VLSHLTSSVE LDFGAAKPIH VTMLPNPSHL EAINPVAQGK TRARQQLRQE GDYSPEENAQ
PGDQVVCLQV HGDGAFPGQG VVPETLTLSN LPHYRVGGSI HLIVNNQVGY TTPSERGRSS
LYCSDVGKMV NCAVIHVNGD EAEDVLRATR LAVEYQRLFR KDVILDLICY RQWGHNELDE
PFFTNPAMYK IIRSRKSVPD SYSDRLISEG LMTEAERDEI KSKHFAVLND KLSISTQYSP
PPTNLQGRWG HLVEPQARVT TWDTGVPVPL LQFIGVKSVD IPEQVQLHSH LRKTHVQARL
QKLEEGTKLD WSTAEALAFG SLLSQGFNIR ISGQDVGRGT FSQRHAMVVC QDTNDMYIPL
NHISAQQTGF LEVCNSPLSE EAVLGFEYGM SIAQPKLLPI WEAQFGDFFN GAQIIFDTFL
TGGEAKWLLQ SGMVILLPHG YDGAGPEHSS CRMERFLQMC DSKEEGVDSD CVNMAVVNPT
TSAQYFHLLR RQMIRNFRKP LIVVGPKMLL RFSGAASSLT ELAPGTCFKP VLGDTSVPAE
SVQKVVLCSG KHYYALLKQR ETSAAKQNTA VVRVEELCPF PLDALQQELT RYPNAKEFVW
SQEEPQNMGP WSFVAPRFEK QLACKLRLVS RPALPAPAVG IGTLHHQQQE AILAGTFS
//
