ID A0A016SGE3_9BILA Unreviewed; 1049 AA.
AC A0A016SGE3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=Acey_s0232.g3022 {ECO:0000313|EMBL:EYB89369.1};
GN Synonyms=Acey-ogdh-1 {ECO:0000313|EMBL:EYB89369.1};
GN ORFNames=Y032_0232g3022 {ECO:0000313|EMBL:EYB89369.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB89369.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYB89369.1}.
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DR EMBL; JARK01001568; EYB89369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SGE3; -.
DR Proteomes; UP000024635; 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 Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 671..887
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1049 AA; 117422 MW; B2CBC766402962C1 CRC64;
MHRAGMLCRL ASPSRAATIA ARKASTVKSG SPLAAAAASQ ARKQSTASSV KQEPFMNATS
SVYIEQMYDA WKADPKSVHA SWDAYFRNVE GGAAPGQAYQ APPMTYGAAG VPGVLPTAVP
SNVAVGGGFT MPQLAQSAVL PATGLDMSTS LQSISEHLKV QLLIRSYQTR GHNIADLDPL
GINSADLDDT IPPELELSFY GFGERDLDKE FLLPPTTFIG GEKPSLTLRE ILHRLKQIYC
TTTGVEYMHL NNLEQQDWIR QRFEAPRVTE LSHDQKKVLF KRLIRSTKFE EFLAKKWPSE
KRFGLEGCEV LIPAIKQVID TSSTLGVDSV VIGMPHRGRL NVLANVCRQP LSTILSQFST
LEPADEGSGD VKYHLGVCIE RLNRQSQRKM KIAVVANPSH LEAVDPVVMG KVRAEAFYAG
DSKCDRTMAI LMHGDAAFSG QGVVMETFNL DDLPSYTVHG CIHIVVNNQV GFTTDPRSSR
SSPYCTDVGR VVGCPIFHVN VDDPEAVMHV CNVAAEWRKT FKKDVIIDLV CYRRHGHNEL
DEPMFTQPLM YQKIKQMPTA LEKYQEHIIN EGVANEQYVK DELTKYGQIL EEAYENAQKV
TYVRNRDWLD SPWDDFFKRR DPLKLVSTGI DPDNINHIIE KFGSYPEGFH LHRGLERILK
GRKQMLKDNS LDWACGEALA FGSLLLEGTH VRLSGQDVER GTFSHRHHVL HDQTIDQKTY
NPLNDLKEGQ AEYTVCNSSL SEYAVLGFEL GYSMVDPNSL VIWEAQFGDF ANNAQCVIDQ
FVASGQSKWI RQSGIVMLLP HGYEGMGPEH SSARPERYLQ LCNEDDQIDL DKVAFGGTFE
AQQLHDTNWI VANCTTPANI FHLFRRQVTM PFRKPAVVMT PKSLLRHPLA RSPIEDFMPG
THFQRVIPEV GPPSQNSANV QRLVFCTGKV YYDLVSARKH VGKDDTVAIC RVEQISPFPY
DLIQAECQKY PGAELIWSQE EHKNMGAWGF VQPRFNSLLQ SENRVIQYTG RHPSASPATG
NKFTHLLEQK DMMSRTFDVP KSQLEGFKA
//
