ID A0A267DFF1_9PLAT Unreviewed; 540 AA.
AC A0A267DFF1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig014467g4 {ECO:0000313|EMBL:PAA47447.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA47447.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA47447.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA47447.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA47447.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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}.
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:PAA47447.1}.
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DR EMBL; NIVC01004450; PAA47447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267DFF1; -.
DR STRING; 282301.A0A267DFF1; -.
DR Proteomes; UP000215902; 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 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 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 PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 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 Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 168..381
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA47447.1"
SQ SEQUENCE 540 AA; 61862 MW; 52D25AB6F472E43D CRC64;
PEEVIHVARV AAEWRAKFGK DVVIDLVCYR RNGHNEMDEP MFTQPLMYKK IKEHKNVLQL
YLEKLISEGT VTQAEYDEES QRYDKVCEDA FTNAKSVKGV RNRDWLDSPW DGFFEGRDAM
KAPATSVTLD RLNKIGQVFS TVPQGFKLHP GLKRTLRGRA ELLEHEQADW AMGEAFAFGS
LLTEGYHVRL SGQDVERGTF SHRHHVLHDQ EKDLATYVPL NNIEQGQATY TVCNSSLSEY
AVMGFELGYS LNDPNALIMW EAQFGDFNNT AQCIIDQFVS SGQQKWVRQS GLVLLLPHGY
EGMGPEHSSA RLERFLQMSN DDPDHIPVLD EDFMMQQLHD INWFVCNVTT PANYFHLMRR
QVLLPFRKPL VLMTPKSLLR LPEARSSFAE MTGDSSFQRL IPDQGPPAKA DPKEVVKLLL
CTGKVYYELV KERERTGQDD TIAICRVEQI SPFPYDLVLK ELNKYPFARV QWVQEEHKNM
GSWFYVQPRV NNLIRSHCPD RTHRHVSYAG RPPSASAAAG NKQLHLMEIA QFLKDAMSPV
//
