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Database: UniProt
Entry: S0EYK1_CHTCT
LinkDB: S0EYK1_CHTCT
Original site: S0EYK1_CHTCT 
ID   S0EYK1_CHTCT            Unreviewed;       948 AA.
AC   S0EYK1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=CCALI_01643 {ECO:0000313|EMBL:CCW35458.1};
OS   Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC   Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC   Chthonomonadaceae; Chthonomonas.
OX   NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW35458.1, ECO:0000313|Proteomes:UP000014227};
RN   [1] {ECO:0000313|Proteomes:UP000014227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23976 / ICMP 18418 / T49
RC   {ECO:0000313|Proteomes:UP000014227};
RA   Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA   Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT   "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT   from the Armatimonadetes phylum (formally candidate division OP10).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; HF951689; CCW35458.1; -; Genomic_DNA.
DR   RefSeq; WP_016482991.1; NC_021487.1.
DR   AlphaFoldDB; S0EYK1; -.
DR   STRING; 454171.CP488_02453; -.
DR   KEGG; ccz:CCALI_01643; -.
DR   PATRIC; fig|1303518.3.peg.1689; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_0; -.
DR   InParanoid; S0EYK1; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000014227; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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:CCW35458.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014227};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          579..774
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   948 AA;  106557 MW;  3F7BCE25CD18BFF7 CRC64;
     MPELSLFTGA NLAYVLDLYE RYQRDPESVD PETRAFFEAY PLSSLLEQSV STDLSNKLLD
     AAIATVRLAR YIRQRGHLDA DIDPLHLSPR SSTELELSAH NLTPEILEQL PSSLIGGPIA
     QETTNARDAI ARLRQVYSGT IGYEDEHIQE AKERYWLRDV VESRRFFKDI DAGRKRDLLH
     RLIEVDIFED FLQRTFPGEK RFSIEGTDAL VPMLDEIVRS AAIEGMHEVV MGMAHRGRLN
     VLAHVLGKPY EVILKEFKNN IGGEGTSVSG SNFEGWSGDV KYHLGYSRAF RESGVAEMPI
     TLVPNPSHLE YVNPVVEGHV RAAQERRDAM GRPQQNERAA LPILIHGDAA FCGQGIVAET
     LNLSRLPGYR TGGTIHIILN NQIGFTTLPS EGRSTLYASD LAKGFEIPIV HVNADDPIAC
     IAAARMAFAY REEFGKDFLI DLIGYRRYGH NETDEPRTTQ PRIYALIDAH PRVREIFAHE
     LEKEGIVSRD EAAAMVNEVR ERLRQALDVA SRMENGEENG NGHMPPPEED AIATGVSAET
     LLSLNEAMLE WPSDFHVNPR AVKQFYEPRR QAIHQPRGIY WAHAEALAFA SILADGIPIR
     LTGQDTERGT FDQRRLALYD VETGERYAPL EHLPQARASF AVYNSPLSES AVLGFEYGYS
     VHAPDTLTLW EAQFGDFANG AQVIIDQFIA AGYAKWGQSP SLVLLLPHGY EGQGPEHSSA
     RVERYLQLCA ENNMRVVNCT TAAQYFHVLR RQAALMRHSP KPLVIFTPKS LLRDKNAAAS
     LQELVEGRFQ PVIDDEEARK RANRVTRLIL CSGKVYMNLL YQPSGEPREE VFKEERLAVV
     RVEQLYPFPV EALAKVIGGY PNLRELVWLQ EEPQNMGAWS FMEPRLRALL HKLEVDCPIR
     YIGREESAST AEGSRPRHLV VQERILRAAL SDIPALSLSR REAARIAK
//
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