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Database: UniProt
Entry: A0A194QA39_PAPXU
LinkDB: A0A194QA39_PAPXU
Original site: A0A194QA39_PAPXU 
ID   A0A194QA39_PAPXU        Unreviewed;       921 AA.
AC   A0A194QA39;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Putative 2-oxoglutarate dehydrogenase E1 component DHKTD1-like, mitochondrial {ECO:0000313|EMBL:KPJ02393.1};
GN   ORFNames=RR46_08190 {ECO:0000313|EMBL:KPJ02393.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPJ02393.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPJ02393.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPJ02393.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ02393.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
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; KQ459249; KPJ02393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194QA39; -.
DR   STRING; 66420.A0A194QA39; -.
DR   Proteomes; UP000053268; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          570..773
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   921 AA;  104295 MW;  D0EE01299A2D4684 CRC64;
     MIAFSKVGVR QLIKWKEYSA CQRIKYHSGA GVFGHRPRDI NEADIPESLI VKRYENCRAQ
     QLVNAYRTYG HLKASIDNVD YKNDKRLVKE LDLTRYGLTP QDYVDLGLLY GYDGKQTAQQ
     LVERLENIYC GNISYEFSYL ETEAEREWFA QRIEASSDLI DNERRREILK ELLHSQAWDK
     FLSVKFPTVK RYCCEGAESL LTFFSTLFGL TTAEGVQQVI LGMAHRGKLN VLSGLLKCPP
     VKIFHKFTGK PEFPAEANAA CDISTHLSAS ADITINNKTV RFSLLNNPSH LEAANPVSMG
     KIRSKQLMLK EGDYSEDGSS RMGDKVLNVQ IHGDAAFTGQ GINQETLMLS QAPHFDVGGS
     LHVVVNNQVG FTLPAERGRS CRYVTDLAKA ISVPVIHVNG DHPELVVKAT NIAFEYQRRF
     RKDVFIDYNC FRRWGHNELD DPTFTNPLLY KLIHSRKSIP DLYAARLVSE GLLNQDDVDK
     IFVDYTKYLQ AQFESVNSYT PEVTYYQDQW TGTSPAPKAV ETWDTGVNEE LLKQVGIASV
     TAPNDFNVHS HLAKTHVRNR LNKISDGREI DWATAEALAF GSLLMEGRHV RLCGEDVGRG
     TFSHRHAMLV DQQTENIYVP LNHIHKDQKG FLEVVNSILS EEAVLGYEYG MAYDSPDNLC
     IWEAQFGDFY NGAQIIVDTY IASGEAKWVR SNGLVMLLPH GYDGAASEHS SCRLERFLQL
     TDSKETAPDG EDVCMHVVNP TTPAQYFHLL RRQVVRNYRK PLIVVAPKVL LRLADAVSPL
     SDFMPGTHFK PVIGDTIADP LKVKRVILVS GKHYYELNKE RIKENIEDVA ILRVESLSPF
     PLHALQKELE KYSNARKYIW SQEEHRNMGA WTFVKPRFEN LLGRKLIYAG RAEAATPAVG
     AGTLHRVEVE HVLKEPLYNI K
//
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