ID F1Q5B8_DANRE Unreviewed; 1019 AA.
AC F1Q5B8; A0A8M2BKA2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 3.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040429};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041946};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
DE AltName: Full=Thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00042799};
GN Name=ogdha {ECO:0000313|Ensembl:ENSDARP00000009474,
GN ECO:0000313|RefSeq:XP_005172527.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-2143};
GN Synonyms=im:7045267 {ECO:0000313|RefSeq:XP_005172527.1}, ogdh
GN {ECO:0000313|RefSeq:XP_005172527.1}, wu:fa06d01
GN {ECO:0000313|RefSeq:XP_005172527.1}, wu:fb98a04
GN {ECO:0000313|RefSeq:XP_005172527.1}, zgc:73296
GN {ECO:0000313|RefSeq:XP_005172527.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000009474};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000009474}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000009474};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000009474, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000009474};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_005172527.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005172527.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
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DR EMBL; CU137648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005172527.1; XM_005172470.4.
DR Ensembl; ENSDART00000022242; ENSDARP00000009474; ENSDARG00000034270.
DR Ensembl; ENSDART00000022242.10; ENSDARP00000009474.10; ENSDARG00000034270.9.
DR GeneID; 564552; -.
DR AGR; ZFIN:ZDB-GENE-030131-2143; -.
DR CTD; 564552; -.
DR ZFIN; ZDB-GENE-030131-2143; ogdha.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000000437; Chromosome 8.
DR Bgee; ENSDARG00000034270; Expressed in cardiac ventricle and 37 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0060047; P:heart contraction; IGI:ZFIN.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF7; 2-OXOGLUTARATE DEHYDROGENASE COMPLEX COMPONENT E1; 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; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 1: Evidence at protein level;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1Q5B8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 648..861
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1019 AA; 115313 MW; 7918D97DEC93E5F8 CRC64;
MHRLRTCAAR LRPITASQTA KNLSQQGPAA TPRTFQPLRC FSSPVAAEPF LNGTSSNYVE
EMYYAWLENP KSVHKSWDIF FRNANAGAPP GTAYQSPPPL GVSLAGLAQA QSLVGAQPNV
EKLVEDHLAV QSLIRAYQVM GHHNANLDPL GISCVNFDEA PVATGFQHVG FYGLEESDLD
KVFRLPTTTF IGGDESALPL REIIRRLEMA YCQHIGVEFM FINDLDQCQW IRQKFERPGV
MQFSLEEKRT LLARMVRSTR FEEFLQRKWS SEKRFGLEGC ESLIPALKTI IDKSSENGVD
TVIMGMPHRG RLNVLANVIR KELEQIFCQF DSKLEAADEG SGDVKYHLGM YHRRINRVTN
RNITLSLVAN PSHLEAVNPV VQGKTKAEQF YSGDTDGKRV MSILLHGDAA FAGQGIVYET
FHLSDLPSYT THGTVHVVAN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV
MYVCNVAAEW RATFHKDVVV DLVCYRRNGH NEMDEPMFTQ PLMYKQIKKQ KGVLQKYAEK
LIAEGAVTRQ EYEEEIAKYD KICEEAHSRS KDEKILHIKH WLDSPWPGFF TLDGQPKSIS
CPSTGLPEEE LAQIGQVASS VPVEDFTIHG GLSRILKGRG DMIKNRTVDW ALGEYMAFGS
LLKEGIHVRL SGQDVERGTF SHRHHVLHDQ NVDKRICIPM NHMSPNQAPY TVCNSSLSEY
GVLGFELGFA MASPNALVLW EAQFGDFHNT AQCIIDQFIC PGQAKWVRQN GIVLLLPHGM
EGMGPEHSSA RPERFLQMCN DDPDFNPKIT DDFDVRQLYD CNWIVVNCSN PANYFHVIRR
QILLPFRKPL IVFTPKSLLR HPEAKSNFDQ MLPGTHFQRV ITDDGPPAQN PSEVKRIVFC
TGKIYYELTR ERKARNMENS VAITRIEQLS PFPFDLVRAE TEKFPNADLV WCQEEHKNQG
YYDYVKPRMR TTINRTKPVW YAGREPAAAP ATGNKNTHLL ELKRFLDTAF NLDAFKDHI
//
