ID   A0A061IQ42_CRIGR        Unreviewed;      1019 AA.
AC   A0A061IQ42;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:ENSCGRP00001019185.1,
GN   ECO:0000313|RefSeq:XP_027243974.1};
GN   ORFNames=H671_1g1694 {ECO:0000313|EMBL:ERE90370.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:ERE90370.1, ECO:0000313|Proteomes:UP000030759};
RN   [1] {ECO:0000313|Proteomes:UP000030759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17A/GY {ECO:0000313|Proteomes:UP000030759};
RX   PubMed=23929341; DOI=10.1038/nbt.2645;
RA   Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA   Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA   Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA   Helk B., Mott J.E., Puhler A., Borth N.;
RT   "Chinese hamster genome sequenced from sorted chromosomes.";
RL   Nat. Biotechnol. 31:694-695(2013).
RN   [2] {ECO:0000313|EMBL:ERE90370.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=17A/GY {ECO:0000313|EMBL:ERE90370.1};
RA   Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA   Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA   Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA   Helk B., Mott J.E., Puehler A., Borth N.;
RT   "Chinese hamster genome sequenced from sorted chromosomes.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSCGRP00001019185.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [4] {ECO:0000313|RefSeq:XP_027243974.1}
RP   IDENTIFICATION.
RC   STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027243974.1};
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_027243974.1};
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; KE664067; ERE90370.1; -; Genomic_DNA.
DR   RefSeq; XP_007643461.1; XM_007645271.2.
DR   RefSeq; XP_027243974.1; XM_027388173.2.
DR   Ensembl; ENSCGRT00001023429.1; ENSCGRP00001019185.1; ENSCGRG00001018679.1.
DR   GeneID; 100764862; -.
DR   CTD; 4967; -.
DR   GeneTree; ENSGT00950000183125; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000030759; Unassembled WGS sequence.
DR   Proteomes; UP000694386; Unplaced.
DR   Proteomes; UP001108280; Chromosome 1.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
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   ECO:0000313|EMBL:ERE90370.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          647..861
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1019 AA;  115823 MW;  F478CB3B2A723F82 CRC64;
     MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE
     MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV
     DKLVEDHLAV QSLIRAYQVR GHHIAKLDPL GISCVNFDDA PVTVSSNVGF YGLDESDLDK
     VFHLPTTTFI GGQESALPLR EIIRRLEMAY CQHIGVEFMF INDLEQCQWI RQKFETPGIM
     QFTNEEKRTL LARLVRSTRF EEFLQRKWSS EKRFGLEGCE VLIPALKTII DKSSENGVDY
     VIMGMPHRGR LNVLANVIRK ELEQIFCQFD SKLEAADEGS GDMKYHLGMY HRRINRVTDR
     NITLSLVANP SHLEAADPVV MGKTKAEQFY CGDTEGKKVM SILLHGDAAF AGQGIVYETF
     HLSDLPSYTT HGTVHVVVNN QIGFTTDPRM ARSSPYPTDV ARVVNAPIFH VNSDDPEAVM
     YVCKVAAEWR STFHKDVVVD LVCYRRNGHN EMDEPMFTQP LMYKQIRKQK PVLQKYAELL
     VSQGVVNQPE YEEEISKYDK ICEEAFTRSK DEKILHIKHW LDSPWPGFFT LDGQPRSMSC
     PSTGLEEDVL AHIGNVASSV PVENFTIHGG LSRILKTRKE LVTNRTVDWA LAEYMAFGSL
     LKEGIHVRLS GQDVERGTFS HRHHVLHDQN VDKRTCIPMN HLWPNQAPYT VCNSSLSEYG
     VLGFELGFAM ASPNALVLWE AQFGDFNNMA QCIIDQFICP GQAKWVRQNG IVLLLPHGME
     GMGPEHSSAR PERFLQMCND DPDVLPDLQE DNFDINQLYD CNWIVVNCST PGNFFHVLRR
     QILLPFRKPL IVFTPKSLLR HPEARTNFDE MLPGTHFQRV IPENGPAAQD PNNVKRLLFC
     TGKVYYDLTR ERKARGMEEQ VAITRIEQLS PFPFDLLLKE AQKYPNAELA WCQEEHKNQG
     YYDYVKPRLR TTIDRAKPVW YAGRDPAAAP ATGNKKTHLT ELQRFLDTAF DLEAFKKFS
//

ID   A0A061IPE4_CRIGR        Unreviewed;      1023 AA.
AC   A0A061IPE4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
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:ENSCGRP00001019166.1,
GN   ECO:0000313|RefSeq:XP_027243971.1, ECO:0000313|RefSeq:XP_027243972.1,
GN   ECO:0000313|RefSeq:XP_027243973.1};
GN   ORFNames=H671_1g1694 {ECO:0000313|EMBL:ERE90374.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:ERE90374.1, ECO:0000313|Proteomes:UP000030759};
RN   [1] {ECO:0000313|Proteomes:UP000030759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17A/GY {ECO:0000313|Proteomes:UP000030759};
RX   PubMed=23929341; DOI=10.1038/nbt.2645;
RA   Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA   Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA   Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA   Helk B., Mott J.E., Puhler A., Borth N.;
RT   "Chinese hamster genome sequenced from sorted chromosomes.";
RL   Nat. Biotechnol. 31:694-695(2013).
RN   [2] {ECO:0000313|EMBL:ERE90374.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=17A/GY {ECO:0000313|EMBL:ERE90374.1};
RA   Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA   Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA   Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA   Helk B., Mott J.E., Puehler A., Borth N.;
RT   "Chinese hamster genome sequenced from sorted chromosomes.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSCGRP00001019166.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [4] {ECO:0000313|RefSeq:XP_027243971.1, ECO:0000313|RefSeq:XP_027243972.1}
RP   IDENTIFICATION.
RC   STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027243971.1,
RC   ECO:0000313|RefSeq:XP_027243972.1};
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_027243971.1,
RC   ECO:0000313|RefSeq:XP_027243972.1};
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; KE664067; ERE90374.1; -; Genomic_DNA.
DR   RefSeq; XP_003504806.1; XM_003504758.3.
DR   RefSeq; XP_007613535.1; XM_007615345.1.
DR   RefSeq; XP_007643459.1; XM_007645269.2.
DR   RefSeq; XP_016832285.1; XM_016976796.1.
DR   RefSeq; XP_027243971.1; XM_027388170.2.
DR   RefSeq; XP_027243972.1; XM_027388171.2.
DR   RefSeq; XP_027243973.1; XM_027388172.2.
DR   Ensembl; ENSCGRT00001023410.1; ENSCGRP00001019166.1; ENSCGRG00001018679.1.
DR   GeneID; 100764862; -.
DR   KEGG; cge:100764862; -.
DR   CTD; 4967; -.
DR   GeneTree; ENSGT00950000183125; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000030759; Unassembled WGS sequence.
DR   Proteomes; UP000694386; Unplaced.
DR   Proteomes; UP001108280; Chromosome 1.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
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   ECO:0000313|EMBL:ERE90374.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          651..865
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1023 AA;  116245 MW;  89C05660C803B37E CRC64;
     MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE
     MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV
     DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES
     DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
     PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN
     GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR
     VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
     YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
     EAVMYVCKVA AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
     AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR
     SMSCPSTGLE EDVLAHIGNV ASSVPVENFT IHGGLSRILK TRKELVTNRT VDWALAEYMA
     FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
     SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP
     HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEDNFDIN QLYDCNWIVV NCSTPGNFFH
     VLRRQILLPF RKPLIVFTPK SLLRHPEART NFDEMLPGTH FQRVIPENGP AAQDPNNVKR
     LLFCTGKVYY DLTRERKARG MEEQVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH
     KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLEAFK
     KFS
//