ID E0W368_PEDHC Unreviewed; 1023 AA.
AC E0W368;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN Name=8236952 {ECO:0000313|EnsemblMetazoa:PHUM601630-PA};
GN ORFNames=Phum_PHUM601630 {ECO:0000313|EMBL:EEB20073.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB20073.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB20073.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB20073.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB20073.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM601630-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM601630-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) 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 -!- 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; AAZO01007334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235882; EEB20073.1; -; Genomic_DNA.
DR RefSeq; XP_002432811.1; XM_002432766.1.
DR AlphaFoldDB; E0W368; -.
DR STRING; 121224.E0W368; -.
DR EnsemblMetazoa; PHUM601630-RA; PHUM601630-PA; PHUM601630.
DR GeneID; 8236952; -.
DR KEGG; phu:Phum_PHUM601630; -.
DR CTD; 8236952; -.
DR VEuPathDB; VectorBase:PHUM601630; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_1_1; -.
DR InParanoid; E0W368; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000009046; 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: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; 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:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EEB20073.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 659..872
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1023 AA; 115006 MW; 32D19C27290BB731 CRC64;
MYRARLVLNK ITPILPGGGE FEKFGSWLLQ STASNNGITW THKRHYSAPS VAEPFLNGSS
SAYVEEMYNA WLADPKSVHV SWDAFFRSSS SGAVPGQAYQ GPPSLAEPRA NEYPLSGLLP
VSGGLPGLGG STINEKIIDD HLAVQAIIRS YQIRGHHIAD LDPLGISSAD LDDKHPPELL
YNHYSFEDED MDRIFKLPST TFIGGAKEKS LSLREILKRL ENAYCRHIGC EFMFINSLEQ
CNWIRQRLEV PGVMEMDKDQ KKLILARLTR AHGFEAFLAR KWSSEKRFGL EGCEILIPAM
KQIIDKSTEL GVESIVMGMP HRGRLNVLAN VCRKPLEQIF TQFAALEAAD DGSGDVKYHL
GTYIERLNRV TNKNIRLAVC ANPSHLEAVD PVVQGKTRAE QFYRGDGEGK KVMSMLLHGD
AAFAGQGVVY ETFHLSDLPD YTTHGTIHII VNNQIGFTTD PRYSRSSAYC TDVARVVNAP
IFHVNSDDPE SVIHVCNIAA EWRATFHKDV VIDIVCYRRN GHNEIDEPMF TQPLMYRKIK
KTPPAVQKYA EKLIGEGIVT PEEVKDVKEK YDKICEEALV NSRKETHIKY KDWLDSPWSG
FFEGKDPLKV GPTGIKEDTL IHIGKRVSSP PPNAAEFVIH KGLERILKAR MEMVESKVVD
WALGEAMAFG SLLKEGIHVR LSGQDVERGT FSHRHHVLHH QLVDKATYRP LCNLYPDQAP
YTVCNSSLSE FAVLGFELGY SMTNPNALVC WEAQFGDFNN TAQCIIDQFI SSGQAKWVRQ
SGLVMLLPHG LEGMGPEHSS ARLERFLQMS SDDPDYFPPE SDEFAIRQLH DINWIVANCT
TPANYFHILR RQIALPFRKP LILMTPKSLL RHPEAKSPFS DMMEGTEFKR MIPEDGPASE
NPGAVKKLIF CSGKVYYDLI KQRREKKLES DIAITRLEQL SPFPFDLVKQ ECSKYSNANL
VWTQEEHKNH GPWFYIQPRI QTAINGSRPL GYSGRPSAAS PATGSKPQHL KELAAFLEDS
ISV
//
