ID   E9PDF2_HUMAN            Unreviewed;      1034 AA.
AC   E9PDF2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=OGDH {ECO:0000313|Ensembl:ENSP00000388183.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000388183.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000388183.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [2] {ECO:0007829|PubMed:19608861}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [3] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [4] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [5] {ECO:0007829|PubMed:25944712}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [6] {ECO:0000313|Ensembl:ENSP00000388183.1}
RP   IDENTIFICATION.
RG   Ensembl;
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; AC004859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005249818.1; XM_005249761.3.
DR   AlphaFoldDB; E9PDF2; -.
DR   SMR; E9PDF2; -.
DR   IntAct; E9PDF2; 1.
DR   MassIVE; E9PDF2; -.
DR   MaxQB; E9PDF2; -.
DR   PeptideAtlas; E9PDF2; -.
DR   ProteomicsDB; 19651; -.
DR   Antibodypedia; 13451; 262 antibodies from 27 providers.
DR   Ensembl; ENST00000447398.6; ENSP00000388183.1; ENSG00000105953.16.
DR   UCSC; uc064diu.1; human.
DR   HGNC; HGNC:8124; OGDH.
DR   VEuPathDB; HostDB:ENSG00000105953; -.
DR   GeneTree; ENSGT00950000183125; -.
DR   OrthoDB; 3597773at2759; -.
DR   BioGRID-ORCS; 4967; 389 hits in 1161 CRISPR screens.
DR   ChiTaRS; OGDH; human.
DR   GenomeRNAi; 4967; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000105953; Expressed in apex of heart and 186 other cell types or tissues.
DR   ExpressionAtlas; E9PDF2; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProt.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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|EPD:E9PDF2,
KW   ECO:0007829|MaxQB:E9PDF2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          662..876
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1034 AA;  117244 MW;  2AC4BD2DE7077487 CRC64;
     MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE
     MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV
     DKLVEDHLAV QSLIRAYQVR GHHIAKLDPL GISCVNFDDA PVTVSSNVDL AVFKERLRML
     TVGGFYGLDE SDLDKVFHLP TTTFIGGQES ALPLREIIRR LEMAYCQHIG VEFMFINDLE
     QCQWIRQKFE TPGIMQFTNE EKRTLLARLV RSTRFEEFLQ RKWSSEKRFG LEGCEVLIPA
     LKTIIDKSSE NGVDYVIMGM PHRGRLNVLA NVIRKELEQI FCQFDSKLEA ADEGSGDVKY
     HLGMYHRRIN RVTDRNITLS LVANPSHLEA ADPVVMGKTK AEQFYCGDTE GKKVMSILLH
     GDAAFAGQGI VYETFHLSDL PSYTTHGTVH VVVNNQIGFT TDPRMARSSP YPTDVARVVN
     APIFHVNSDD PEAVMYVCKV AAEWRSTFHK DVVVDLVCYR RNGHNEMDEP MFTQPLMYKQ
     IRKQKPVLQK YAELLVSQGV VNQPEYEEEI SKYDKICEEA FARSKDEKIL HIKHWLDSPW
     PGFFTLDGQP RSMSCPSTGL TEDILTHIGN VASSVPVENF TIHGGLSRIL KTRGEMVKNR
     TVDWALAEYM AFGSLLKEGI HIRLSGQDVE RGTFSHRHHV LHDQNVDKRT CIPMNHLWPN
     QAPYTVCNSS LSEYGVLGFE LGFAMASPNA LVLWEAQFGD FHNTAQCIID QFICPGQAKW
     VRQNGIVLLL PHGMEGMGPE HSSARPERFL QMCNDDPDVL PDLKEANFDI NQLYDCNWVV
     VNCSTPGNFF HVLRRQILLP FRKPLIIFTP KSLLRHPEAR SSFDEMLPGT HFQRVIPEDG
     PAAQNPENVK RLLFCTGKVY YDLTRERKAR DMVGQVAITR IEQLSPFPFD LLLKEVQKYP
     NAELAWCQEE HKNQGYYDYV KPRLRTTISR AKPVWYAGRD PAAAPATGNK KTHLTELQRL
     LDTAFDLDVF KNFS
//