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Database: UniProt
Entry: F0LIT0_THEBM
LinkDB: F0LIT0_THEBM
Original site: F0LIT0_THEBM 
ID   F0LIT0_THEBM            Unreviewed;       311 AA.
AC   F0LIT0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Ketoisovalerate oxidoreductase VorB-like subunit {ECO:0000313|EMBL:ADT84532.1};
GN   OrderedLocusNames=TERMP_01557 {ECO:0000313|EMBL:ADT84532.1};
OS   Thermococcus barophilus (strain DSM 11836 / MP).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT84532.1, ECO:0000313|Proteomes:UP000007478};
RN   [1] {ECO:0000313|EMBL:ADT84532.1, ECO:0000313|Proteomes:UP000007478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX   PubMed=21217005; DOI=10.1128/JB.01490-10;
RA   Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT   "Complete genome sequence of the hyperthermophilic, piezophilic,
RT   heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL   J. Bacteriol. 193:1481-1482(2011).
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; CP002372; ADT84532.1; -; Genomic_DNA.
DR   RefSeq; WP_013467830.1; NC_014804.1.
DR   AlphaFoldDB; F0LIT0; -.
DR   GeneID; 26137245; -.
DR   KEGG; tba:TERMP_01557; -.
DR   PATRIC; fig|391623.17.peg.1557; -.
DR   eggNOG; arCOG01601; Archaea.
DR   HOGENOM; CLU_058423_0_0_2; -.
DR   OrthoDB; 296931at2157; -.
DR   Proteomes; UP000007478; 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:UP000007478}.
FT   DOMAIN          92..218
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   311 AA;  34689 MW;  78A5FE546B9B0AFC CRC64;
     MEIPENIKKR LSIPFEENFY AGHTACQGCG AALGLRYVLK AYGKKAIFTI PACCSTIIAG
     PWPYSAFGAP LFHTAFETTG AVISGIEAAL KAKGYKVKGK DGIMVVGWAG DGGTADIGLQ
     ALSGFLERGH DALYIMYDNE AYMNTGIQRS SSTPYGAWTT NTPGGKKHFL EKRHKKKVID
     IVIAHKIPYA ATASIAFPED FMRKLKKAQE IPGPSFIQLF APCPTGWRSP TDKSIELARL
     AVQTAYFPLF EYENGKYKIN MPNPKKEPKP IEEFLKLQGR FKYMTKEDIE ILQEWVLREW
     EELKKKAEVF G
//
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