ID   A0A1H3F8C0_ALLWA        Unreviewed;       957 AA.
AC   A0A1H3F8C0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=SAMN05421644_11710 {ECO:0000313|EMBL:SDX87222.1};
OS   Allochromatium warmingii (Chromatium warmingii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=61595 {ECO:0000313|EMBL:SDX87222.1, ECO:0000313|Proteomes:UP000198672};
RN   [1] {ECO:0000313|Proteomes:UP000198672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 173 {ECO:0000313|Proteomes:UP000198672};
RA   Varghese N., Submissions S.;
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; FNOW01000017; SDX87222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3F8C0; -.
DR   STRING; 61595.SAMN05421644_11710; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000198672; 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:UP000198672};
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   957 AA;  107531 MW;  50F91C1D52ED8729 CRC64;
     MSTLLDLLRG SSALYGGNAA FIEDLYERYL LDPDSIDPAW RVRFDQWRQR VTPGTRTVET
     PHTPIRERFR QLAETTPTQA ARSTPRCLDP VAAEKQAAVL SLINAYRYRG HQIADIDPIR
     LREVPHVADL DLAYHHLLPA DLDQVFHTGS LYAPDRLTLR EILDIVQETY GGTVGSEYMH
     ITSTQEKRWI QKRLEGYRAR PELDSEGRRW LLTLLTAAEG LEKYLHQRYV GQKRFSLEGG
     EALIPLLDEL VQRAGRRGMQ EIVIGMAHRG RLNVLTNIFG KPPADIFDEF EGRVQLDWRQ
     MVGDVKYHMG FATDVATPGG IVHLVLGFNP SHLEIINPVV EGSVRARQRR RGDRSGDQVL
     PVLIHGDAAF AGQGVVMETL QLSQTRSYGT GGTVHIVINN QIGFTTSHPL DARSTPYCTD
     VAKMVQAPVF HVNGDDPEAV IFVTRLALDF RNQFHKDVII DLMCYRRLGH NEADEPAVTQ
     PLMYQKIREH PTPRAIYAER LLMHGLITPE DEQALITAYR QALEQGVVIA RAVLCGLDTS
     RRVDWRFCRG QSWDQDIDTG VPLDTLRTLS TALLRLPEGF VLHPRVEKVW EERQKMAQGE
     QLLNWGYAEN LAYATLLAEG IPVRLSGQDV GRGTFVHRHA KLYDQVTGAA YTPLQHLSEQ
     QGAFIAIDSI LSEEAVLGYE YGFATAEPHA LTLWEAQFGD FANGAQVVID QFISSAGTKW
     GLHCGLVMLL PHGLEGQGAE HSSARLERFL QLCAGHNMQV CVPTTPAQLF HLLRRQMVRP
     YRTPLIVMTP KSLLRHRLAV SALDELTQGQ YQVIIPESDP IDPAEVERVV LCSGKVYYDL
     LEARRARGRN QVALLRIEQL YPFPKAAFVQ ALEPYAHVEE IVWCQEEPQN QGAWDQIKHR
     LQRLLPAGKR AYYVGRPASA APAVGHRAAH VEQHERLIEA ALGGAPNSNP NLRIPSP
//