ID   A0A1H4DJF7_9GAMM        Unreviewed;       948 AA.
AC   A0A1H4DJF7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=SAMN05660964_02263 {ECO:0000313|EMBL:SEA72676.1};
OS   Thiothrix caldifontis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=525918 {ECO:0000313|EMBL:SEA72676.1, ECO:0000313|Proteomes:UP000199397};
RN   [1] {ECO:0000313|EMBL:SEA72676.1, ECO:0000313|Proteomes:UP000199397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21228 {ECO:0000313|EMBL:SEA72676.1,
RC   ECO:0000313|Proteomes:UP000199397};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNQP01000012; SEA72676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4DJF7; -.
DR   STRING; 525918.SAMN05660964_02263; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000199397; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000199397};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          603..796
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   948 AA;  105700 MW;  475DE8E20775C796 CRC64;
     MNKGEAQATA WNADTQLDGN SLLYLEEMYE RYLQEPASIP ASWQHYFDAL PAVNGHERDT
     RHSLVKDYFR AYAAKPQAVA APVAGSVDME HERKQVKVLQ LINAYRFLGH FHAKTNPLDE
     NTPAFVKELT LAYHSLSEAD LDTTFNTGSL VAPDQLTLRE IIAQLEATYC GSIGVQYMHT
     TSTEQKRWVQ QRLESVRSTP TFSPAEKLEI LDRLTAAEGL ERYLHTNYVG QKRFSLEGGE
     SLIPMLNTLI QHGGSLGAQE MVIGMAHRGR LNVLVNVLGK APALLFGEFE GKYANNGDRT
     GDVKYHMGFA SDMMTPGGPL HVAMAFNPSH LEIVGPVVQG AVRARQDRWD DAGGDKIIPV
     VLHGDAAFAG QGVNMEMLQM ADTRGYRTYG TIHIVINNQV GFTTSTAADA RSTYYCTDIA
     KMVDSPVFHV NGDDPEAVVL ITQIAFDFRA KFDKDVVIDL VCYRRHGHNE ADEPSATQPV
     MYRKIRALPT TRELYARRLT GEGLITAEDA QERVQRCRQQ LTSGAPTVPH LLEKGEVQNP
     HPVKWKRFVD NAWDMPVDTT ISADAVKRLG TKLTEYPADF KLNSRVARIV ADRKKMAAGE
     QLMDWGFCEN LAYASLIDEG YPIRLSGEDC GRGTFFHRHA VFHEQESGAT FVPLQHLSEA
     QMPFVVIDSL LSEEAVLAFE YGYATTEANT LVIWEAQFGD FANCAQVVID QFISSGEQKW
     GRLCGLVMLL PHGFEGQGPE HSSARLERYL QLCAQHNMQV CVPSTPAQAF HMLRRQMVRD
     YRTPLIVMTP KSLLRHPLAV NSMEDLTERG FQNVIDEIDV LDPLKVTRLV MCSGKVYYDL
     LEQRRKAGLD DVALVRIEQI YPFPEADMNV ILDRYPNIAV NVWCQEEPLN QGAWLSIQPA
     LRLVLGGMAR LDVVSRPASA SPAVGSAKVH AAQQQELVNN ALGIRVES
//