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Database: UniProt
Entry: W4VJI6_9BACI
LinkDB: W4VJI6_9BACI
Original site: W4VJI6_9BACI 
ID   W4VJI6_9BACI            Unreviewed;       593 AA.
AC   W4VJI6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:GAE93382.1};
GN   ORFNames=JCM21714_2462 {ECO:0000313|EMBL:GAE93382.1};
OS   Gracilibacillus boraciitolerans JCM 21714.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=1298598 {ECO:0000313|EMBL:GAE93382.1, ECO:0000313|Proteomes:UP000019102};
RN   [1] {ECO:0000313|EMBL:GAE93382.1, ECO:0000313|Proteomes:UP000019102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21714 {ECO:0000313|EMBL:GAE93382.1,
RC   ECO:0000313|Proteomes:UP000019102};
RA   Ahmed I., Oshima K., Suda W., Kitamura K., Iida T., Ohmori Y., Fujiwara T.,
RA   Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of the Boron-Tolerant and Moderately Halotolerant
RT   Bacterium Gracilibacillus boraciitolerans JCM 21714T.";
RL   Genome Announc. 2:e00097-14(2014).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE93382.1}.
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DR   EMBL; BAVS01000012; GAE93382.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4VJI6; -.
DR   STRING; 1298598.JCM21714_2462; -.
DR   eggNOG; COG0567; Bacteria.
DR   Proteomes; UP000019102; 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   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   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   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 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:UP000019102};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          235..431
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   593 AA;  66913 MW;  6357F77F85316DE5 CRC64;
     MGDAAFIGEG VVAETFNLSA LPGYHTGGTL HIIANNLVGF TTGQRQGRST RYASDLAKGF
     EVPIIHVNAD DPEACISATI LAYDYRKKFK KDILIDLVGY RRYGHNEMDE PRATQPKLYE
     SIDNHPTCAT VYAKRLVQDG ILNENTHEEM KESVFNKLQG IYDDMTENIN ENPEVMPLPQ
     ALRQGLSDIE TAVPKDLLHS LNKGLLKRPE GFQSFKKLEK ILTKRHNTFT EEEKADWAVG
     EALAYASIIQ DGIPIRMTGQ DSERGTFAHR HLMLHDVETS ETYCPMHGLD EAKSTFDIHN
     SPLSEAAVLG FEYGYSVKAP KTLVIWEAQF GDFANAGQVI FDQFISSSRA KWDERSNMVM
     LLPHGYEGQG PEHSSARVER FLTMAAENNW IVANVTTSAQ FFHLIRRQAA LVNSEAARPL
     IVLTPKSLLR SPRVVSAIEE FANEKFKPLM PQPGLNLTSK KAKRLLIGTG KVMVDIAEKM
     DENPQKYENL HVLRLEQMYP FPERQIQEVL DGCPNLKEVV WVQEEPRNMG AWNFVKELLY
     KMLENSDLEL HYEGRCERSA PSVGDAHIHK AEQRRIIKRA VEWSEGGDTN EGN
//
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