ID   L0E2I9_THIND            Unreviewed;       926 AA.
AC   L0E2I9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA [H] {ECO:0000313|EMBL:AGA35410.1};
GN   OrderedLocusNames=TVNIR_3784 {ECO:0000313|EMBL:AGA35410.1};
OS   Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA35410.1, ECO:0000313|Proteomes:UP000010809};
RN   [1] {ECO:0000313|Proteomes:UP000010809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC   {ECO:0000313|Proteomes:UP000010809};
RA   Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA   Ravin N.V., Popov V.O.;
RT   "Complete sequence of Thioalkalivibrio nitratireducens.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003989; AGA35410.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0E2I9; -.
DR   STRING; 1255043.TVNIR_3784; -.
DR   KEGG; tni:TVNIR_3784; -.
DR   PATRIC; fig|1255043.3.peg.3819; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000010809; 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:AGA35410.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          573..766
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   926 AA;  103802 MW;  095A243EBAD61BC7 CRC64;
     MLRRMDLHPD SLAFAEALFE RYRNDPDAVP AAWADYFGAL QRETAPSASA AGDCIDERDL
     QLERLQVRVL QYINAYRFLG HFAARLDPLQ RNLPETPPEL TRAYHELDRV DPAQTFDPGS
     LHGPSPARLD EIEEILQDTY CACIGAEFMH LTSTAEKRWL QQRLESARGH FGFDPDTQQA
     ILERITAAEG LERYLHHRYV GQKRFSLEGA ESLIPLLNAL VQRGGARGVK EIVVGMAHRG
     RLNVLVNVFG KSPRELADEF EGRPSRNRGT GDVKYHLGYS SDVQTPGGAV HLALAFNPSH
     LEIVTPVVEG SVRARQVRLG DRQGRKVMPV VIHGDAAFAG QGVVMETLNM AQTRGFSTKG
     TVHIVANNQI GFTTSTLKDS RSTHYSTDVA KMVSAPIMHV NGDDPEAVVF VTQLALDYRM
     RFGKDVVIDL VCYRRQGHNE ADEPAATQPM MYRIIRELPT TREHYARRLV EQGVIEESMA
     QRLQERYRDS LESGESVVPG LLSPDEADGH KPTNWGPFVN QAWDQDIETG VPREQLSSLL
     ERLNRLPEGF VVHPRVRRIL EARTAMAVAE QPLDWGTAET LAYATLLQDG YRVRMSGQDS
     GRGTFFHRHA VLHDQETGQS LVPLRQLDSE DPRFLVIDSL LSEEAVLAFE YGYATAAPNA
     LVLWEAQFGD FANGAQVVID QFISSGEQKW GRLCGLVLLL PHGYEGQGPE HSSARPERFL
     QLCAQENMQV CVPTTPAQIF HLLRRQLVRP YRKPLVVMTP KSLLRHKFAV SDLDDLASGG
     FELVIDDIDR PDPADVRRVI LTSGRIYYDL LGEKRDAGHD DVAILRVEQC YPFPDAVLTR
     LLGRYDQASE FVWVQDEPEN QGYLGFMEPR LNALLEVRGQ RLHAVARPAA AAPAVGYPEV
     HKAQQQELMR RSFGPITARD TPRPTE
//