ID A0A286ZWR6_PIG Unreviewed; 978 AA.
AC A0A286ZWR6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=OGDHL {ECO:0000313|Ensembl:ENSSSCP00000036125.2,
GN ECO:0000313|VGNC:VGNC:98169};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000036125.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000036125.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000036125.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000036125.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:ARBA00043712};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000256|ARBA:ARBA00043712};
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; A0A286ZWR6; -.
DR SMR; A0A286ZWR6; -.
DR STRING; 9823.ENSSSCP00000036125; -.
DR Ensembl; ENSSSCT00000043899.3; ENSSSCP00000036125.2; ENSSSCG00000010394.5.
DR VGNC; VGNC:98169; OGDHL.
DR GeneTree; ENSGT00950000183125; -.
DR InParanoid; A0A286ZWR6; -.
DR Proteomes; UP000008227; Chromosome 14.
DR Bgee; ENSSSCG00000010394; Expressed in oocyte and 21 other cell types or tissues.
DR ExpressionAtlas; A0A286ZWR6; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; 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 NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF5; 2-OXOGLUTARATE DEHYDROGENASE-LIKE, MITOCHONDRIAL; 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; 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 1: Evidence at protein level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZWR6};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 621..818
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 17..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 110641 MW; 1B61359C10A100B7 CRC64;
MQDTGIPSWR IFALSDSGNL MPEPSAPRTA PPGRAGSSGP PATFPSSRVG GGSSYMEEMY
FAWLENPQSV HKSWDSFFRK ASEEASYGLA QPRPPSVVPE SRPAASGRTK TSKLVEDHLI
RGHHVAQLDP LGILDADLDS FVPSDLITTI DKLAFYDLQE ADLDKEFQLP TTTFIGGSEH
TLSLREIIRR LESTYCQHIG LEFMFINDVE QCQWIRQKFE TPGVIPSILA LLSPSRFEDF
LARKWSSEKR FGLEGCEVMI PALKTIIDKS SEMGIENVIL GMPHRGRLNV LANVIRKDLE
QIFCQFDPKL EAGSGDVKYH LGMYHERINR VTNRNITLSL VANPSHLEAV DPVVQGKTKA
EQFYRGDAQG KKVMSILVHG DAAFAGQGVV YETFHLSDLP SYTTNGTVHV VVNNQIGFTT
DPRMARSSPY PTDVARVVNA PIFHVNADDP EAVIYVCSVA AEWRNTFNKD VVVDLVCYRR
RGHNEMDEPM FTQPLMYKQI HRQVPVLKKY ADKLIAEGTV TLQEFEEEIA KYDRICEEAY
GRSKDKKILH IKHWLDSPWP GFFNVDGEPK SMTCPATGIP EDVLTHIGEV ASSVPLEDFK
IHTGLSRILR GREDMTRKRT VDWALAEYMA FGSLLKEGIH VRLSGQDVER GTFSHRHHVL
HDQEVDRRTC VPMNHLWPDQ APYTVCNSSL SEYGVLGFEL GYAMASPNAL VLWEAQFGDF
HNTAQCIIDQ FISTGQAKWV RHNGIVLLLP HGMEGMGPEH SSARPERFLQ MSNDDSDAYP
AFTQDFEVRQ LYDCNWIVIL LPFRKPLIIF TPKSLLRHPE AKSSFDQWYQ VWTSFQRVIP
EDGAAVRAPE QVQRLIFCTG KVYYDLVKER SNQGLDEQVA ITRLEQISPF PFDLIKQEAE
KYPGAELVWC QEEHKNMGYY DYISPRFMTI LGRARPIWYV GRDPAAAPAT GNRNTHLVSL
KKFLDTAFNL QAFDGKTF
//
