ID A0A2A2K517_9BILA Unreviewed; 867 AA.
AC A0A2A2K517;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=WR25_13925 {ECO:0000313|EMBL:PAV69018.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV69018.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV69018.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV69018.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV69018.1}.
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DR EMBL; LIAE01009632; PAV69017.1; -; Genomic_DNA.
DR EMBL; LIAE01009632; PAV69018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2K517; -.
DR STRING; 2018661.A0A2A2K517; -.
DR Proteomes; UP000218231; 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; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; 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; PF00676; E1_dh; 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:UP000218231};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 553..758
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 867 AA; 98594 MW; 654B34AD10ED6DA3 CRC64;
MVIYEKDRTL GVSHRFYRPG ADEFGHLPDP PKSSFEPTGS ITDENCRNVH LINAYRRYGY
LQADLDPLGL EKKKDVPELN PELYGAKPDD ALSSSNDLQV NDLAEQLRLI YCGTMAVEFM
HINNWEERQW IAQHFEEAVA TELRSEERVK LAKLMLRCEN FDHFLGQKFP TLKRYSGEGA
EAQFGFFSEI FDSAPEHGLQ QILVGIAHRG RNNLLVEMMQ FPYVQMFRKI RGKPELPEGV
QGSGDVLSHL VSSFDHETSD GKVHITMLPN PSHLEAQNPV AMGKARARAR SLNIGDYSKG
RDARVGDGVL CLLVHGDGSF TGQGVVWESI ALSQAPHFRL GGVIHLVTNN QIAFTAESHI
GRSSRHCTDI AKAFEYPVLH VNGDKPEDLV KATRLAMAYR EKFRKDIFIN LICFRKWGHN
ELDDPTFTNP LLYKVINSRE SVPREYADEL IGDELITEEE VKKLKDDHTG KLLEAYRAVD
GTPPKVNHLN GYWKGIVQAP SEVQTWDTGV DLELLRYVGA QTVKVPEKFN LHEHLKKTHI
DARIQKLTSG EGIDWSTAEA LAFGSLLVEG NDVRISGQDV GRATFCHRHA IMVDQETDQS
HIPFNCIDPN QKGFLEVVNN LLSEEAILGF EFGFAIDNPK RLCIWEAQFG DFNNGAQIII
DTFIASAESK WLTQSGLTML LPHGYDGAGP EHSSCRMERF LQLCDSKEDQ QPVDGENINM
RVVNPSTSAQ YFHLLRRQVV PNYRKPCIVV APKILLRHPK VSILKKPIFL KYVARNIGFT
HEIFCSIYCS FVKQTIIYLK PSNLKKVHEQ MRKLDMFRLV WYENKSKHKL QGSNRGIKII
IAGRFISDRI CPWYSFQERH RRFDVQG
//