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Database: UniProt/TrEMBL
Entry: C6A488_THESM
LinkDB: C6A488_THESM
Original site: C6A488_THESM 
ID   C6A488_THESM            Unreviewed;       393 AA.
AC   C6A488;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=2-ketoisovalerate:ferredoxin oxidoreductase (VOR) subunit alpha {ECO:0000313|EMBL:ACS90433.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:ACS90433.1};
GN   OrderedLocusNames=TSIB_1382 {ECO:0000313|EMBL:ACS90433.1};
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS90433.1, ECO:0000313|Proteomes:UP000009079};
RN   [1] {ECO:0000313|EMBL:ACS90433.1, ECO:0000313|Proteomes:UP000009079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX   PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS90433.1; -; Genomic_DNA.
DR   RefSeq; WP_015849651.1; NC_012883.1.
DR   AlphaFoldDB; C6A488; -.
DR   STRING; 604354.TSIB_1382; -.
DR   GeneID; 8096384; -.
DR   KEGG; tsi:TSIB_1382; -.
DR   eggNOG; arCOG01608; Archaea.
DR   HOGENOM; CLU_002569_5_0_2; -.
DR   OrthoDB; 372068at2157; -.
DR   Proteomes; UP000009079; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ACS90433.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009079}.
FT   DOMAIN          15..240
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          263..366
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   393 AA;  44122 MW;  92098FE527879357 CRC64;
     MPKKVISGNY AAAYAAKHAR VEVVAAYPIT PQTSIIEKIA EFIANGEVEN LEYVPVESEH
     SAMAACIGAS AAGARTFTAT SAQGLALMHE MLHWAAGARL PVVMVDVNRA MAPPWSVWDD
     QTDSLAQRDT GWLQFYAENN QEVYDGVLMA FKIGEHEKVN LPVMVIESAF ILSHTYDIVD
     MLEQEEVDEF LPPRKPLYSL TDFDNPFSIG ALGTPADYYE FRYKIAKAME EAKKIIKEVG
     KEFGEKFGRD YSQMIELYKT EDADIVFMGM GSLMGTVKEA VDIFRSEGYK VGAAKVRWFR
     PFPREELYEL AKSVEGIAVL DRNFSFGQEG ILFNEAKGIL YNTDANPIMK NYIVGLGGRD
     LTVNDVRKIA SNMKKIIEKG ELDKEIDWYH LKR
//
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