ID E3JXA4_PUCGT Unreviewed; 1133 AA.
AC E3JXA4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN ORFNames=PGTG_02140 {ECO:0000313|EMBL:EFP76679.2};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP76679.2, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
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 EMBL; DS178266; EFP76679.2; -; Genomic_DNA.
DR RefSeq; XP_003321098.2; XM_003321050.2.
DR AlphaFoldDB; E3JXA4; -.
DR STRING; 418459.E3JXA4; -.
DR EnsemblFungi; EFP76679; EFP76679; PGTG_02140.
DR GeneID; 10528618; -.
DR KEGG; pgr:PGTG_02140; -.
DR VEuPathDB; FungiDB:PGTG_02140; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; E3JXA4; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0006103; P:2-oxoglutarate metabolic process; IEA:EnsemblFungi.
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:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 763..977
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1133 AA; 126240 MW; 9AA4EEE13AD09B4E CRC64;
MPIVGSDRLS HPYTQVSPGL FSFGPKGNAG SEAEECLGCL GSAWIPGFDR GRVCCAGEIA
YSPALPSTPT APHSYSTTSH KNQQTKQINI SPLSVSRTTH CPLATVLGNC HSVIMHRLNL
NKIASAPRFL SNSLAPSNRL TSKFTKSSQN LRHLATATND QVLRKAPSPV DGFVNSNNSY
YIEEMYRMWR KDPGSVHASW NVYFSGLEKG LPSENAFRPP PGLVSMPQPA GGAPMLAMPG
SGGEVEDHMK IQLLVRAYQV RGHHIAKLDP LNLSEADLQT IRPPEMDLKH YGFDENTDYE
KEFSLGPGIL PLFHTKDREK MKLREIIEAC NRIYCGHIGL QYVHLPDRKE CDWIRERVEL
PVPWSYSLEE KRMILDRLIW SDSFERFVAS KHPNEKRFGL EGGESLIPGM KALIDRSVDA
GVKSIVIGMP HRGRLNVLSN VVRKPMEAIF NEFAGSADAS EDGGGDVKYH LGANYVRPTP
SGKKVALSLV ANPSHLEAED PVVLGKTKAL QHFDGEGSTD HAMGILLHGD AAFAGQGVVY
ETMGFHDLPH FGTGGTVHLV INNQIGFTTD PRQGRSTPYC TDIAKSIDAP IFHVNGDDAE
AVTFVCQLAA DWRAAFKKDV VVDIVCYRRH GHNETDQPSF TQPKMYQAIG QQPPTLKIYT
DHLIKEGSFT EQENQQSQRM GVEYDGEGLR RKSGLQPNFA RVAVELELKE NILEARPTGV
ERSVMNKIGD TISGGWPENF EVHKNLGRIL KNRGKTIAEG DQIDWSTAEA LAFGSLLLEG
NHVRVSGQDV ERGTFSQRHA VLHDQKTNDN YIPLSNLKPE GSDPVGPFTI CNSSLSEFGA
LGFELGYSLV DPHLLTMWEA QFGDFANNAQ CIIDQFICSG ERKWLQRTGL VMSLPHGYDG
QGPEHSSARI ERFLQLCDDD PFKFPTPEKA QRIHQDCNMQ LVYCTTPSNY FHVLRRQIHR
DFRKPLIVFF SKSLLRHPLA KSSVTEMEPG TFFIPLIPEP GFSGMVENHQ IKRHIFCSGQ
VYYTLLQERE KRNINDIAIT RIEQLSPVPY YEIVKALETY PNSDVMYCQE EPVNGGAYTY
LAPRLENAMN QTENHAGKKV LYAGRPPYAS VATGSKKIHK QEVQQFLDQA LNV
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