ID J9BIF9_WUCBA Unreviewed; 994 AA.
AC J9BIF9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
DE Flags: Fragment;
GN ORFNames=WUBG_01931 {ECO:0000313|EMBL:EJW87160.1};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW87160.1, ECO:0000313|Proteomes:UP000004810};
RN [1] {ECO:0000313|Proteomes:UP000004810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Wuchereria bancrofti.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:EJW87160.1}.
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DR EMBL; ADBV01000476; EJW87160.1; -; Genomic_DNA.
DR AlphaFoldDB; J9BIF9; -.
DR Proteomes; UP000004810; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 663..879
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 994
FT /evidence="ECO:0000313|EMBL:EJW87160.1"
SQ SEQUENCE 994 AA; 112528 MW; D684858CCC85DF3E CRC64;
MLRRTGFLKN KASLKFLGCL KCTSYTLSKS NLMRKQCIIS GLRQKFAATS VKEEPFMNGT
STVYIEQMYE AWRQSPTSVH SSWNAYFQNV ERSLPPGQAY SAPPKGLASY SVSSAVAPAP
EFENALNVSG QTIDEHLKVQ LLIRSYQTRG HNIADLDPLG INNVGLTDIT PAELDPAFYG
LADTDMDKEF LLPMSTFIGG DKKSLKLRDI ISRLKTIYCS HTGIEYMHLT NFEQLEWVRK
RFEEPCASEL THEQKKTLFK RLIRSTKFEE FLAKKWPSEK RFGLEGCEVL IPAAKQVIDV
SSAAGVDSVV IGMPHRGRLN MLANVCRQPL SVILSQFSTL EPADEGSGDV KYHLGISLER
LNRVSGRKLK LLSLRIHLIL KVSLRSFSGA NKGKTVDPIV LGKVRAESFY NGDENGDHTM
AILLHGDAAF SGQGVVMETF NLNDLKGYTT HGTIHLVVNN QIGFTTDPRC SRSSPYCTDI
GRVVGCPIFH VNSDDPEAVM HVCNVAADWR RTFKKDVIID LVCYRRYGHN ELDEPMFTQP
LMYQRVRKTK PVLAIYQKQI LAENVVNEQY VEDEVNKYNT LLEDAYQEAQ KVAYLRHRDW
IDSPWDTFFK KRDPLKIPAT GVAKEMISHI IEKFSSVPAD FNLHRGLDRI LKGRRQMFQD
NSFDWAMGEA VAFGSLLLEG THVRLSGQDV ERGTFSHRHH VLHDQKIDQK TYNPLDNLSD
KQAEYSISNS SLSEFAILGF ELGYSMVNPN SLVIWEAQFG DFANNAQCIT DQFLSSGQSK
WIRQSGLVMS LPHGYEGMGP EHSSARLERF LQMSNEDDEI DVDHTAFGPT FEAQQLYDTN
WIVVHCTTPS NFCHLLRRQV MLPFRKPLII MSPKSLLRHP SARSPIEDFL PGTKFCRVVP
EGGSASQDPD KVERLVFCTG KVYYDLMSAR KHLNLDSRIA ISRVEQISPF PYDLIEKECL
KYSKAELIWA QEEHKNMGAW GFVHPRLGAL IAKF
//
