ID   A0A0L8GY99_OCTBM        Unreviewed;       921 AA.
AC   A0A0L8GY99;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=OCBIM_22025941mg {ECO:0000313|EMBL:KOF81943.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF81943.1};
RN   [1] {ECO:0000313|EMBL:KOF81943.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF81943.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF81943.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ419930; KOF81943.1; -; Genomic_DNA.
DR   RefSeq; XP_014777041.1; XM_014921555.1.
DR   AlphaFoldDB; A0A0L8GY99; -.
DR   STRING; 37653.A0A0L8GY99; -.
DR   EnsemblMetazoa; Ocbimv22025941m; Ocbimv22025941m.p; Ocbimv22025941m.g.
DR   EnsemblMetazoa; XM_014921555.1; XP_014777041.1; LOC106874001.
DR   GeneID; 106874001; -.
DR   KEGG; obi:106874001; -.
DR   OMA; TPAQYYH; -.
DR   OrthoDB; 3597773at2759; -.
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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          573..776
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   921 AA;  103663 MW;  6E13E6E4791F43A1 CRC64;
     MLMLPRRLLR QNWLATKLQS TAAYHSKSGV YGYRPRNKST SEEVLCSETI ENRIKHSNAY
     ALVQNYRRYG HKLAKLDPLG LKETQSIQQL NPSRYGFSGD NEVADINVKG ILHCGYGYQS
     PKELIENLQR QYCGHIGAEF EHLENEVERE WFAHAFETKD SIEVSAERQI SLAKLMLRCQ
     AFDQFLASKF TTVKRYGGEG CESMMAAFDE IFSRSSQYGV TDIVMCMPHR GRLNFLTTML
     DFPPVRMFRK MKGLTELPPM AKGSGDVLSH LYTSQDLKYG DNSVHVSLIP NPSHLEANNP
     VAVGKARAKI QSLKIGDYGH DGVTQNKDVL CFQVHGDASF SAQGIISETF SFAECAHFSV
     GGSIHLIVNN QIGFTTEAER GRSSMYCSDQ AKINGYPVLH VNADDPKAII QAAAIAVDYR
     QQFHRDIIID LVCFRRWGHN ELDDPMFTQP IMYKAVESRM SIPDMYAQQL TQQDLCTESE
     LKSFVQEWNN VLVENFNKTD SYIPEQFHLL KQWDGYVQAS DNITSWDTGV DVDVLKFIGD
     KSVTVPETTN VHPTIQKTHI DRRKKQIEAG IDLDWATAES LAIGSLLYQG FNVRISGQDV
     GRGTFSHRHA MIVDQKSDDI YIPLNHISSD QVGCFEAANS VLSEEAVLGF EYGMSLEHPK
     NLVIWEAQFG DFFNGAQPII DTYVTSGETK WLLQSGLVML LPHGFDGAGP EHSSCRIERF
     LQLCDSKEDA IDSDHVNMEI VHPTTSGQYF HLLRRQMVRN YRKPLIVAAP KTLLRLSSAA
     SSLLDMAPGT CYQPVLGDNK VNPESVTRLV FCSGKHFYAL NKQRDASNSH NVAIIRLESL
     CPFPVADLLK EIKKYPKAKE FIWSQEEHRN MGPWSFVAPR FQNLLACKLN YVGRGTLASA
     AVGIATEHQK EAQQLIAATF Q
//