ID L5K9Z3_PTEAL Unreviewed; 1117 AA.
AC L5K9Z3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=PAL_GLEAN10004430 {ECO:0000313|EMBL:ELK08350.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK08350.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043712};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000256|ARBA:ARBA00043712};
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; KB030894; ELK08350.1; -; Genomic_DNA.
DR STRING; 9402.L5K9Z3; -.
DR eggNOG; KOG0450; Eukaryota.
DR InParanoid; L5K9Z3; -.
DR Proteomes; UP000010552; 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; IPR032106; 2-oxogl_dehyd_N.
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 PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF5; 2-OXOGLUTARATE DEHYDROGENASE-LIKE, MITOCHONDRIAL; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 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:UP000010552};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 736..949
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1117 AA; 126834 MW; F7E89A3A194DC147 CRC64;
MSQLRLLPSR LGAQATRILT PHNVQMFSWH SRSSGPPATF PSSKGGGSSS YMEEMYFAWL
ENPQSVHKSW DSFFRKASEE GSCVPAQPLL SFLVPESRPA VSSRTKTSKL VEDHLAVQSL
IRAYQIRGHH VAQLDPLGIL DADLDSFVPS DLITTIDKLA FYDLREADLD KEFRLPMTTF
IGGSEHTLSL REIIRRLEST YCQHIGLEFM FINDVEQCQW IRQKFETPGV MRFSSEEKRT
LLARLVRSMR FEDFLARKWS SEKRFGLEGC EVMIPALKTI IDKSSEMGIE NVILGMPHRG
RLNVLANVIR KDLEQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRVTN RNIALSLVAS
PSHLEAVDPV VQGKTKAEQF YRGDAQGKKV MSILVHGDAA FAGQGVVYET FHLSDLPSYT
TNGTVHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV IYVCSVAAEW
RNTFNKDVVV DLVCYRRRGH NEMDEPMFTQ PLMYKQIHRQ MPVLKKYADK LISEGTVTLQ
EFEEEIAKYD RICEEAYGKS KDKKILHIKH WLDSPWPGFF NVDGEPKSMT CPATXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXIPEDVLS HIGDVASSVP LEDFKIHTGL
SRILRSRADM TKKRTVDWAL AEYMAFGSLL KEGIHVRLSG QDVERGTFSH RHHVLHDQEI
DRRTCVPMNH LWPDQAPYTV CNSSLSEYGV LGFELGYAMA SPNALVLWEA QFGDFHNTAQ
CIIDQFISTG QAKWVRHNGI VLLLPHGMEG MGPEHSSARP ERFLQMSNDD SDAYPTFTKD
FEVSQLYDCN WIVVNCSTPA SYFHVLRRQI LLPFRKPLII FTPKSLLRHP EAKSNFDHML
CGTSFQRVIP EDGAAAQAPE QVRRLIFCTG KVYYDLVKER SSQGLEEQVA ITRLEQVHLV
RMMDKISPFP FDLIMQEAEK YPSAELVWCQ EEHKNMGYYD YISPRFMTIL SRARPIWYVG
RDPAAAPATG NRNTHLVSLK KFLDTAFNLQ AFEGKTF
//
