ID   Q97AF0_THEVO            Unreviewed;       629 AA.
AC   Q97AF0;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=2-ketovalerate ferredoxin oxidoreductase [VOR] alpha subunit {ECO:0000313|EMBL:BAB60002.1};
GN   ORFNames=TVG0881751 {ECO:0000313|EMBL:BAB60002.1};
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116 {ECO:0000313|EMBL:BAB60002.1, ECO:0000313|Proteomes:UP000001017};
RN   [1] {ECO:0000313|EMBL:BAB60002.1, ECO:0000313|Proteomes:UP000001017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1
RC   {ECO:0000313|Proteomes:UP000001017};
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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DR   EMBL; BA000011; BAB60002.1; -; Genomic_DNA.
DR   RefSeq; WP_010917104.1; NC_002689.2.
DR   AlphaFoldDB; Q97AF0; -.
DR   STRING; 273116.gene:9381652; -.
DR   PaxDb; 273116-14325077; -.
DR   DNASU; 1441952; -.
DR   GeneID; 1441952; -.
DR   KEGG; tvo:TVG0881751; -.
DR   eggNOG; arCOG01606; Archaea.
DR   HOGENOM; CLU_017038_1_0_2; -.
DR   OrthoDB; 31112at2157; -.
DR   PhylomeDB; Q97AF0; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   CDD; cd17039; Ubl_ubiquitin_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03710; OAFO_sf; 1.
DR   NCBIfam; NF041170; Oxoac_fdxalpha_Archa; 1.
DR   PANTHER; PTHR32154:SF16; PYRUVATE FLAVODOXIN_FERREDOXIN OXIDOREDUCTASE DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317}.
FT   DOMAIN          12..209
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          243..487
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          514..604
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   629 AA;  69214 MW;  33EAF01938717D9B CRC64;
     MDFNILIGGP QGGGIDTAAN LVGKAVATSG YGVLSVREYH SNIKGRHSYT HMRVKEDQPR
     SLKYPVNIFV ALDPDTIFEH LDDVSEASIV IYDKTTEDYD LQAARMIMRD TSAKIRSILQ
     ENGFETTIRG ALKYMQKRGA KLLPVPFADI ATQAVPNGTP SRYFNTIGAA IALAIIGIDE
     KFAKDSISYI FRGKQQVVEE NVKVVEQSYK FATDSGVAGK TLPAKPTPRK LLLTGNDASA
     LGKLLGGLRF QTYYPITPAS DESTTLEEHQ NIKWLKNEAE SLKKGGVVIV QTEDELSAIN
     MAIGGALTGA RSATATSGPG FSLMAEGLSF AGMDEVPLVV TFYERGGPST GLPTRNGQSD
     LLFALNAGHG EYPRIVFSSG TVDECIYDAV KALNYAAKYQ MPVIHLIDKN LANTLDLISK
     IDLDKVKIEK VELAKEGDDV KRYDLNTQNG VSPYAVMGRN IFWMTGDEHD ELGHVTEDSD
     IRDRMMEKRF KKLETADKEI PVDEKAQLIG PEDADITFVT WGSQKGPILD VIEDLKQDDI
     TANLLYLKMF SPFPTEFVKS ILSKAHLVID VESNFTAQAA QMIKLYTGIE IENKILKYNG
     RHMTEDEILN SAKNILNKKS LMVVLEDGS
//