ID   A0A1I7RT42_BURXY        Unreviewed;       906 AA.
AC   A0A1I7RT42;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=(pine wood nematode) hypothetical protein {ECO:0000313|EMBL:CAD5231452.1};
GN   ORFNames=BXYJ_LOCUS11548 {ECO:0000313|EMBL:CAD5231452.1};
OS   Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS   xylophilus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC   Bursaphelenchus.
OX   NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0389600.1};
RN   [1] {ECO:0000313|WBParaSite:BXY_0389600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:CAD5231452.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5231452.1};
RA   Kikuchi T.;
RL   Submitted (SEP-2020) 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; CAJFDI010000005; CAD5231452.1; -; Genomic_DNA.
DR   EMBL; CAJFCV020000005; CAG9122626.1; -; Genomic_DNA.
DR   WBParaSite; BXY_0389600.1; BXY_0389600.1; BXY_0389600.
DR   eggNOG; KOG0451; Eukaryota.
DR   Proteomes; UP000095284; Unplaced.
DR   Proteomes; UP000582659; Unassembled WGS sequence.
DR   Proteomes; UP000659654; 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; -; 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; 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; 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:UP000659654};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          554..759
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   906 AA;  101902 MW;  861EB76D3F3B49DC CRC64;
     MNRFHRLSPI RLGGSRRSYH FRQSIFGFSD KSPAGKNNLI EIDQTIQSPK DLCDLYQKYG
     YRAANLDPLG LWDNSGNKKL LREFAATLDA QNISHGDFSG RLDEFISYLE TTYCNDLAIE
     FKHLNSVKEQ KWIADEFEKI KRTEFSRDEK KKIAESMLKA LAFEKFLEAK IPTLKRYSGE
     GAEAAVVFHE RLLKDGPKYN IKELIWGGAH RGRMALHTVL FGLEPDTVLR KIRGLPEFPD
     NVDGSGDVLS HLNCHYDVET ADGKIHVSTA PNPSHLEVAG PVAVGKSRGR ALTLHVGDYG
     ETTVGDEILC VHYHGDGAFS GQGVVWETLS MAQVPHFRIG GSIHLVANNQ VAFTAEKDIG
     RSSLHCTDYA KALDCPVIHV NACSSEDASR AAELALKYRQ EFRKDVFVNL HCFRRHGHNE
     IDNPRFTNPL LYKKVDAMED IPDVYASKLV EDGVVDAGFG EKVKRDYQSY LNDSLTRVDS
     GRSEPKADHL QGYWAGYQQA PKAVTVYSTG LNTDLLRYVG ARSVNVPDGF KVHPHILKTH
     INARLQRLEK SEHIDWATAE AFAFGSLLLQ GYDVRISGQD VGRATFSHRH GVLVDQETDE
     IYIPLNNITD GQKSFFEAAN SPLSEEAILG FEYGFSIENP RRLVIWEAQF GDFYNTAQVQ
     IDTLIASGES KWLIQSGLVL VLPHGIDGAG PDHSSSHMER FLQLTDSRED QRPVDGDNVN
     MHVVNPTTSA QYFHLLRRQC LTPFRKPLII ISPKVLLRHP MAASPLSDFE EGTFFKPVLD
     DVDSKPEKVK KVVFVTGKHA VLLMTERTKR GLEDTAIVRL ERLCPFPVSE VREVLKKYSN
     ASNFIWSQEE PKNAGAWSFI RPRFENALGL QLKYVGRPEL AWMATSIGQH HQKEADKVLQ
     DTFQTS
//