ID A0A180G5T4_PUCT1 Unreviewed; 1027 AA.
AC A0A180G5T4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=PTTG_04398 {ECO:0000313|EMBL:OAV88047.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV88047.1};
RN [1] {ECO:0000313|EMBL:OAV88047.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV88047.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV88047.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV88047.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAV88047.1}.
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DR EMBL; ADAS02000220; OAV88047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180G5T4; -.
DR STRING; 630390.A0A180G5T4; -.
DR VEuPathDB; FungiDB:PTTG_04398; -.
DR OrthoDB; 3597773at2759; -.
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: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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 657..871
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1027 AA; 115660 MW; 00CEBF396B377049 CRC64;
MHRLNLNKLT SAPRFLSNSL TPSNRLTSRF TKSSQNLRQL ATATNDQVLR KAPSPVDGFV
NSNNSYYIEE MYRMWRKDPS SVHASWNVYF SGLEKGLPSE LAFRPPPGLV SMPQPAGGAP
MLAMPGSGGE VEDHMKIQLL VRAYQVRGHH IAKLDPLNLS EADLETLRPP EMDLKHYGFD
ENTDYDKEFS LGPGILPLFH TKDREKMKLR EIIDACNRIY CGHIGLQYVH LPDRKECDWI
RERVELPVPW SYSLEEKRMI LDRLIWSDSF ERFVASKHPN EKRFGLEGGE SLIPGMKALI
DRSVDAGVKS IVIGMPHRGR LNVLSNVVRK PMEAIFNEFA GSADASEDGG GDVKYHLGAN
YVRPTPSGKK VALSLVANPS HLEAEDPVVL GKTKALQHFD GEGSTDHAMG ILLHGDAAFA
GQGVVYETMG FHDLPHFGTG GTVHLVINNQ IGFTTDPRQG RSTPYCTDIA KSIDAPIFHV
NGDDVEAVTF VCQLAADWRA AFKKDVVVDI VCYRRHGHNE TDQPSFTQPK MYQAIGKQPS
TLKIYTDHLI KEGSFSEQEI NNHKEWVWGM MEKAYEGSQH YNPTSREWLS SSWDGFPSPK
ELKENILEAR PTGVERSVMN KIGETISGGW PENFEVHKNL GRILKTRGKT IAEDDQIDWS
TAEALAFGSL LLEGNHVRVS GQDVERGTFS QRHAVLHDQN TNENYIPLSN LKPEGSDPVG
PFTICNSSLS EFGALGFELG YSLVDPHLLT MWEAQFGDFA NNAQCIIDQF ICSGERKWLQ
RTGLVMSLPH GYDGQGPEHS SARIERFLQL CDDDPFKFPT PEKAQRIHQD CNMQLVYCTT
PSNYFHVLRR QIHRDFRKPL IVFFSKSLLR HPLAKSSISE MEPGTFFIPL LPEPGFSGMV
DNHQVKRHIF CSGQVYYTLV QEREKRNINN VAITRLEQLS PVPYYEIVKA LETYPNSDVM
YCQEEPINSG AYSYLAPRLE NVMNQTENHA GKKVLYAGRP PYASVATGSK KIHKQEIQQF
LDQAFNV
//
