ID   Q8PS99_METMA            Unreviewed;       481 AA.
AC   Q8PS99;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   02-SEP-2026, entry version 120.
DE   SubName: Full=Ketoisovalerate oxidoreductase subunit {ECO:0000313|EMBL:AAM32879.1};
GN   Name=vorA {ECO:0000313|EMBL:AAM32879.1};
GN   OrderedLocusNames=MM_3183 {ECO:0000313|EMBL:AAM32879.1};
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM32879.1, ECO:0000313|Proteomes:UP000000595};
RN   [1] {ECO:0000313|EMBL:AAM32879.1, ECO:0000313|Proteomes:UP000000595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC   {ECO:0000313|Proteomes:UP000000595};
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA   Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA   Fritz H.J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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DR   EMBL; AE008384; AAM32879.1; -; Genomic_DNA.
DR   RefSeq; WP_011035078.1; NC_003901.1.
DR   AlphaFoldDB; Q8PS99; -.
DR   SMR; Q8PS99; -.
DR   DNASU; 1481525; -.
DR   GeneID; 24864609; -.
DR   KEGG; mma:MM_3183; -.
DR   PATRIC; fig|192952.21.peg.3696; -.
DR   eggNOG; arCOG01600; Archaea.
DR   HOGENOM; CLU_042621_1_1_2; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-ARBA.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IEA:UniProtKB-ARBA.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR051457; 2-oxoacid:Fd_oxidoreductase.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   PANTHER; PTHR48084:SF3; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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:UP000000595}.
FT   DOMAIN          76..226
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          305..473
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
SQ   SEQUENCE   481 AA;  51588 MW;  7B573997B4E8359C CRC64;
     MAAEIINGEK VIRKPNALYS DYPRKGGAAS TATHYCPGCG HGVLHKLIAE AIDDLGIQDR
     TVMISPVGCA VFAYYYFDTG NIQVAHGRAP AVGTGVSRAE ENAVVISYQG DGDLASIGLN
     ETLQAANRGE KIAVFFVNNT VYGMTGGQMA PTTLIGEKTT TTPEGRDPRF AGYPLHMCEL
     LDNLKAPVFI ERVSVSDISH IRKARKAIRK ALEVQRDGKG YAFVEVLAAC PTNLRMDAEQ
     AVSFINEEME KEFPLRNFRD DSESTEPLYR GVSDFTTESL EKLYGIEADA GEKPVRADFA
     PIQTKIAGFG GQGVLSMGIV LAQAGVKANL NASWFPSYGP EQRGGTSNCS VVISGQPIGS
     PTVYTPDILI AMNRPSLERF EGAVRKGGFI LYDSTIGEAE TPEGVKAVSV PATEKAKEAG
     DERAANSFML GVLLGLNATG LEEEAFKGAL AENFAGKPRV IAFNQQMLEA GAEWARENVK
     I
//