ID A0A183JB58_9BILA Unreviewed; 174 AA.
AC A0A183JB58;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Transket_pyr domain-containing protein {ECO:0000313|WBParaSite:SBAD_0001352201-mRNA-1};
GN ORFNames=SBAD_LOCUS13106 {ECO:0000313|EMBL:VDP54151.1};
OS Soboliphyme baturini.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0001352201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SBAD_0001352201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP54151.1, ECO:0000313|Proteomes:UP000270296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UZAM01020283; VDP54151.1; -; Genomic_DNA.
DR WBParaSite; SBAD_0001352201-mRNA-1; SBAD_0001352201-mRNA-1; SBAD_0001352201.
DR Proteomes; UP000050793; Unplaced.
DR Proteomes; UP000270296; 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 Gene3D; 3.40.50.12470; -; 2.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000270296};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 31..74
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|Pfam:PF02779"
SQ SEQUENCE 174 AA; 20049 MW; B58B2465DC1636AC CRC64;
MSNVPEGFEI HPGLKRILRM RAEMMANQTS DWALGEAFAF GSLLKEGIHV RLGGQDVERG
TFSHRHHVLH DQKVDKKVYV PLQDLSPLRI RFATVLYQNT PFWDLKSVSR XXXXXXXXXX
XXXXXXXXXX XXXNALVIWE AQFGDFANNA QCIFDQIISR YCITTVYFWP HQII
//
