ID A0A1V9XWN3_9ACAR Unreviewed; 859 AA.
AC A0A1V9XWN3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative 2-oxoglutarate dehydrogenase E1 component DHKTD1 {ECO:0000313|EMBL:OQR77890.1};
GN ORFNames=BIW11_02835 {ECO:0000313|EMBL:OQR77890.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR77890.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR77890.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR77890.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(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:OQR77890.1}.
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DR EMBL; MNPL01002910; OQR77890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XWN3; -.
DR STRING; 418985.A0A1V9XWN3; -.
DR InParanoid; A0A1V9XWN3; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000192247; 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 InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
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; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 2.
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:UP000192247};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 544..747
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 859 AA; 97262 MW; FF014F107EDBC46E CRC64;
MIFRATKVIR RQVLRTFSSN TRISPDDYRI HMLADSIRRH GHLRANVNPF KNVKTTLHSP
WVEKMTPEDF GLPRNGLLEY GGQTGSIDEW YKRMLATYTG HVGVEFMHLE SERREWFIKM
LEKEAFLSAK PLQEFQKQIC KTLLESQTFD NFLAAKFATV KRYGGEGAEC MNAFFLQLLL
QAPICGITDI MIAIPHRGRL NLLTGLLQFP TETVFRKMRG LSEFEISKYP TATGDVLSHL
FTSVRIQENL RISLLPNPSH LEATCPVVVG KARARLQQLL GNHRYSQVCD APRHNNPWVL
PIQVHGDASF AGQGVVMETL LLSRLPYFKA GGSLHLIVNN QIGYTTPSAF GKSSNYNSDV
MKSIDAPVLH VNGDHPEAVC VATQLALNYR QHFGQDVLVD MWCFRRWGHN EMDDPTFTNP
IMYREIHARQ SVPDLYAQKL QDEGVITKGE VTAIVSSHNA RLTKSLAAAD SYESRTQTLR
DRWSNIVPAP REGLMRFNTG LPTELLQYIG LKSTEVPTDF NVHPHLKKVV IAERAKRFTE
GKRLDWAMAE LLAFGSLLYQ GHNVRISGQD VGRGTFSQRH VMLFDNETEE SHITLNSLRP
DQGLLEVVNS PLSEEAVLSF EYGFSLESPN NLVIWEAQFG DFHNSAQVVL DTLVTSGERK
WLLQTGMTIL LPHGYDGAGP EHSSSRIERF LQICDSNEQG APDTEDVNFR FANPTTAAQY
FHLLRRQILP NFRKPLIVAS PKIILRLPEA SSTFMDMAPE AKRQQLRRTD IAIIRLEQLC
PFPVADLAEA LRPFQHVKDF VWAQEEGRNM GPWFFVAPRM KNFFNIEMSY CGRRPLGTPA
VGVGSFHKAE AAALLDSIF
//
