ID F7FVJ6_MONDO Unreviewed; 923 AA.
AC F7FVJ6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=2-oxoadipate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040865};
DE AltName: Full=2-oxoadipate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041619};
DE AltName: Full=Alpha-ketoadipate dehydrogenase {ECO:0000256|ARBA:ARBA00042817};
DE AltName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042094};
DE AltName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial {ECO:0000256|ARBA:ARBA00042537};
GN Name=DHTKD1 {ECO:0000313|Ensembl:ENSMODP00000020972.3};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000020972.3, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000020972.3, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000020972.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoadipate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-glutaryldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:69576, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:17726, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57499, ChEBI:CHEBI:83099, ChEBI:CHEBI:184385;
CC Evidence={ECO:0000256|ARBA:ARBA00043772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC Evidence={ECO:0000256|ARBA:ARBA00043772};
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 RefSeq; XP_001367890.1; XM_001367853.2.
DR AlphaFoldDB; F7FVJ6; -.
DR STRING; 13616.ENSMODP00000020972; -.
DR Ensembl; ENSMODT00000021342.4; ENSMODP00000020972.3; ENSMODG00000016802.4.
DR GeneID; 100013507; -.
DR KEGG; mdo:100013507; -.
DR CTD; 55526; -.
DR eggNOG; KOG0451; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_0_0_1; -.
DR InParanoid; F7FVJ6; -.
DR OMA; TPAQYYH; -.
DR OrthoDB; 3597773at2759; -.
DR TreeFam; TF314198; -.
DR Proteomes; UP000002280; Chromosome 8.
DR Bgee; ENSMODG00000016802; Expressed in liver and 19 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
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; 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:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 573..776
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 923 AA; 103819 MW; EC202A951A03C7C6 CRC64;
MAYSVTAAAA VARRNLEWIP RQLLRRGYQT ERGVYGYRPK QRENGEPRGG TARSAVDHGL
ARLVTAYCEH GHKAAKINPL FAGQAVMENV PEIQTLVETL QGPFNTTGLL SMGKEEASLE
EVLAYLNHIY CGQISMETIQ LQSQEEKDWF ASRFEELKKE TFTTEEKKHL SRLMLESQEF
DHFLATKFAT VKRYGGEGAE SMMGFFHELL KMAAYSGVTD VIIGMPHRGR LNLLTGLLQF
PPELMFRKMR GLSEFPESIS ATGDVLSHLT SSVDLDFGSH RPLHVTMLPN PSHLEAVNPV
AVGKTRGRQQ SQLDGDYSPD SAAQPGDKVI CLQVHGDASF CGQGIVPETF TLSNLPHFRI
GGSIHLIVNN QLGYTTPAER GRSSLYCSDI GKIVGCAVIH VNGDNPEEVV RATRLAMEYQ
RQFRKDIIVD LLCYRQWGHN ELDEPFFTNP VMYKIIRSRK SIPDTYAESL IAHGLMTQEE
VSEIKNSYYS KLSDHLTNMT LYSPPATNLQ AHWRGLVEPS ARITTWDTGV PIDLLRFVGG
KSVEVPEELQ MHSHLLKTYV QARIEKIKEG MKLDWATAEA LALGSLLAQG FNVRLSGQDV
GRGTFSQRHA MIVCQNTDDM YIPLNHMDAD QKGFLEVSNS PLSEEAVLGF EYGMSIESPK
LLPIWEAQFG DFFNGAQIIF DTFISGGESK WLLQSGIVIL LPHGYDGAGP DHSSCRMERF
LQMCDSVEEG VDGDNVNMFV VHPTTPAQYF HLLRRQMIRN FRKPLIVASP KMLLRFPAAV
SSFQEMAPRT TFRPVIGDSS VDPKNVKSIV FCSGKHFYAL MKQRENLEEK KDNYAIIRIE
ELCPFPLEAL QQELSKYRNA KDFIWSQEEP QNMGPWFFIS PRFEKQLACK LRLVSRPPLP
APAVGIGTIH QQQQEEILTK TFA
//
