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Database: UniProt
Entry: Q5JIJ9_THEKO
LinkDB: Q5JIJ9_THEKO
Original site: Q5JIJ9_THEKO 
ID   Q5JIJ9_THEKO            Unreviewed;       311 AA.
AC   Q5JIJ9;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=2-oxoisovalerate:ferredoxin oxidoreductase, beta subunit {ECO:0000313|EMBL:BAD86170.1};
GN   OrderedLocusNames=TK1981 {ECO:0000313|EMBL:BAD86170.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD86170.1, ECO:0000313|Proteomes:UP000000536};
RN   [1] {ECO:0000313|EMBL:BAD86170.1, ECO:0000313|Proteomes:UP000000536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC   {ECO:0000313|Proteomes:UP000000536};
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain. {ECO:0000256|ARBA:ARBA00011595}.
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DR   EMBL; AP006878; BAD86170.1; -; Genomic_DNA.
DR   RefSeq; WP_011250931.1; NC_006624.1.
DR   AlphaFoldDB; Q5JIJ9; -.
DR   STRING; 69014.TK1981; -.
DR   EnsemblBacteria; BAD86170; BAD86170; TK1981.
DR   GeneID; 78448516; -.
DR   KEGG; tko:TK1981; -.
DR   PATRIC; fig|69014.16.peg.1935; -.
DR   eggNOG; arCOG01601; Archaea.
DR   HOGENOM; CLU_058423_0_0_2; -.
DR   InParanoid; Q5JIJ9; -.
DR   OrthoDB; 296931at2157; -.
DR   PhylomeDB; Q5JIJ9; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR   CDD; cd03376; TPP_PFOR_porB_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000536}.
FT   DOMAIN          92..218
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   311 AA;  34602 MW;  E62747FE4E490CCF CRC64;
     MEIPEQIKKK LTLPAEEHFY AGHTACQGCG AALGLRYVLK AYGRKTIFAI PACCSTIIAG
     AWPYNTLGAN LFQTAFETTG AVLGGIEAAL KARGIKVKGE DGVMIVGWAG DGGTADIGLQ
     ALSGFLERGH DALYIMYDNE AYMNTGIQRS SSTPYGAWTT NTPGGKRHFL EKRHKKKVID
     IVIAHEIPYA ATASVAYPED FIRKLKTAQK TPGPSFIQLF APCPTGWRSP TDKSIEIARL
     AVQTAYFPLF EYKEGKYRIN MPNPKKEPKP IEEFLKLQGR FKYMTKEDIQ VLQEWVLREW
     EKLKKLAEVF G
//
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