ID C4K9S0_THASP Unreviewed; 949 AA.
AC C4K9S0;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=Tmz1t_2544 {ECO:0000313|EMBL:ACR01146.1};
OS Thauera aminoaromatica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=164330 {ECO:0000313|EMBL:ACR01146.1, ECO:0000313|Proteomes:UP000002186};
RN [1] {ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR01146.1, ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|EMBL:ACR01146.1,
RC ECO:0000313|Proteomes:UP000002186};
RX PubMed=23407619; DOI=10.4056/sigs.2696029;
RA Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL Stand. Genomic Sci. 6:325-335(2012).
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP001281; ACR01146.1; -; Genomic_DNA.
DR RefSeq; WP_012585555.1; NC_011662.2.
DR AlphaFoldDB; C4K9S0; -.
DR STRING; 85643.Tmz1t_2544; -.
DR KEGG; tmz:Tmz1t_2544; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_4; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000002186; Chromosome.
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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACR01146.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002186};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 592..789
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 949 AA; 106860 MW; 6B39BCD8ED2C0C81 CRC64;
MMKQLEQTSH LFGSNAPFIE EQYENYLADP ASVSAEWREY FDKLQVQVGA AARDVPHGPV
IAAFEQMAKR GPVRTIVTAG EDKQQVSVLQ LINAYRFLGN RWANLDPLKR TERPQIAELE
PSYYGFTEAD LSKSFNVGSF HGFSTERATL REILEALRQT YCGSIGAEYM YMTDIGQKRW
IQSRLESLRG TPKFSAEMKK RILERTTAAE TLERYLHTRY VGQKRFSLEG GESAIVAMDE
LIRVAGSLGV QESVIGMAHR GRLNVLVNTL GKSPSMLFSE FEGKAAADLT AGDVKYHMGF
SSDVMTPGGP MHLTLAFNPS HLEIINPVVE GSVYARQVRR GDADKKQVLP VLIHGDAAVA
GQGVNQEMLN FSQTRGYGTG GTVHLVVNNQ IGFTTSDPRD YRSSLYCTDI FKMVEAPIFH
VNGDDPEAVA LVTALAVEFR QEFKKDVVVD IICFRKLGHN EQDEPMVTQP LMYRTIQKHP
GTRKLYAERL VAEGTLKAEE PDQMIAEYRE HLDKGQLLYN PVLSGHNRQF AADWTPYIKQ
PYTDECDTTV PVQEIKRLSE RLSTIPANFT LHSRVKKIID DRAAMGRGEA PFDWGMGENL
AYASLLAQGY GVRLSGEDVG RGTFFHRHAV LHDQKRERWD EGIYKPLDHI QDGQARFQSY
DSVLSEEGVL AFEYGYATTE PNELVIWEAQ FGDFVNGAQV VLDQFISSGE AKWGRLCGLT
LMLPHGYEGQ GPEHSSARLE RYMNNAAEHN WQICVPTTPA QIFHLLRRQA IRKVRKPLII
ITPKSLLRHK EAISSIEELA NGSFQTVIPE VEKLDAKKVK RVVLCQGKIY YELLAHRREN
KITDTALVRI EQLYPFPTEA FAKAIEQFPN AKEIVWAQEE PRNQGAWYWL ASRQHLVNVL
GTKRRLLLVS RPAAASPAVG YYAKHNAQQK AVLENAFGPI QDTTPQSPH
//
