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Database: UniProt
Entry: A0A2A2K517_9BILA
LinkDB: A0A2A2K517_9BILA
Original site: A0A2A2K517_9BILA 
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
//
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