GenomeNet

Database: UniProt
Entry: A0A096P498_PAPAN
LinkDB: A0A096P498_PAPAN
Original site: A0A096P498_PAPAN 
ID   A0A096P498_PAPAN        Unreviewed;       994 AA.
AC   A0A096P498;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=OGDHL {ECO:0000313|Ensembl:ENSPANP00000020173.3};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000020173.3, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000020173.3, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000020173.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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:ARBA00033699};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC         Evidence={ECO:0000256|ARBA:ARBA00033699};
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   AlphaFoldDB; A0A096P498; -.
DR   Ensembl; ENSPANT00000019325.3; ENSPANP00000020173.3; ENSPANG00000022654.3.
DR   eggNOG; KOG0450; Eukaryota.
DR   GeneTree; ENSGT00950000183125; -.
DR   HOGENOM; CLU_004709_1_1_1; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000028761; Chromosome 11.
DR   Bgee; ENSPANG00000022654; Expressed in lateral hypothalamic nucleus and 44 other cell types or tissues.
DR   ExpressionAtlas; A0A096P498; baseline.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProt.
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:UP000028761};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          622..835
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          106..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   994 AA;  112778 MW;  9CC765729B86B552 CRC64;
     MSGQWLGRAS SCLSPVVYAS PSLPVSRMNQ LRLLPSRLGA QAVRLLAAHE VPVFGWRSRS
     SGPPATLPSS KDGGSSSYME EMYFAWLENP RSVHKSWDNF FRKASEEASS GSAQPRPPSV
     VRDSRSAVSS RTKTSKLVED HLAVQSLIRA YQIRGHHVAQ LDPLGILDAD LDSFVPSDLI
     TTIDKLAFYD LQEADLDKEF QLPTTTFIGG SENTLSLREI IRRLENTYCQ HIGLEFMFIN
     DVEQCQWIRQ KFETPGVMQF SSEEKRTLLA RLVRSMRFED FLARKWSSEK RFGLEGCEVM
     IPALKTIIDK SSEMGIENVI LGMPHRGRLN VLANVIRKDL EQIFCQFDPK LEAADEGSGD
     VKYHLGMYHE RINRVTNRNI TLSLVANPSH LEAVDPVVQG KTKAEQFYRG DAQGKKVMSI
     LVHGDAAFAG QGVVYETFHL SDLPSYTTNG TVHVVVNNQI GFTTDPRMAR SSPYPTDVAR
     VVNAPIFHVN ADDPEAVIYV CSVAAEWRNT FNKDVVVDLV CYRRRGHNEM DEPMFTQPLM
     YKQIHRQVPV LKKYADKLIA EGTVTLQEFE EEIAKYDRIC EEAYGRSKDK KILHIKHWLD
     SPWPGLSRIL RGRADMTKNR TVDWALAEYM AFGSLLKEGI HVRLSGQDVE RGTFSHRHHV
     LHDQEVDRRT CVPMNHLWPD QAPYTVCNSS LSEYGVLGFE LGYAMASPNA LVLWEAQFGD
     FHNTAQCIID QFISTGQAKW VRHNGIVLLL PHGMEGMGPE HSSARPERFL QMSNDDSDAY
     PAFTKDFEVS QLYDCNWIVV NCSTPANYFH VLRRQILLPF RKPLIIFTPK SLLRHPEAKS
     SFDQMVSGTS FQRVIPEDGA AAQAPEQVQR LIFCTGKVYY DLVKERSSQG LEEKVAITRL
     EQISPFPFDL IKQEAEKYPG AELAWCQEEH KNMGYYDYIS PRFMTILRRT RPIWYVGRDP
     AAAPATGNRN THLVSLKKFL DTAFNLQAFE GKTF
//
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