ID G7VDH3_9CREN Unreviewed; 301 AA.
AC G7VDH3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=P186_1329 {ECO:0000313|EMBL:AET32758.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET32758.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET32758.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET32758.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342; EC=1.2.7.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000005};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000256|ARBA:ARBA00011631}.
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DR EMBL; CP003098; AET32758.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VDH3; -.
DR STRING; 1104324.P186_1329; -.
DR KEGG; pyr:P186_1329; -.
DR eggNOG; arCOG01601; Archaea.
DR HOGENOM; CLU_058423_0_0_2; -.
DR OrthoDB; 296931at2157; -.
DR BioCyc; PSP1104324:GJSN-1303-MONOMER; -.
DR Proteomes; UP000005867; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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:SF1; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR PANTHER; PTHR42897; 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;
FT DOMAIN 69..202
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 301 AA; 32816 MW; 16E8E3379366A090 CRC64;
MSFRIDQLPK KKYVVPGNAA CAGCGMMIGW KILGMALGEE AVLTIPASCA AVVQGLSPKS
GVAMPILNVP FASAAAVATG IAEAYRSLGV KGHAVVWAGD GGTSDIGFAT LSGAAERNSN
IIYIMYDNEA YMNTGIQRSS STPLAAWTTT TPMGKRERKK DVALLMAMHG VPYVATASIA
YPQDFYRKLK RAAEVEGFKF IHLHTPCPPG WRFDPAKTVE VARLAVETGV WILWEYDHGH
FRLNPPSTTY ADKAKRRPLI EYLKLQGRFA HVTEEQVKAL EEDVEARWRS ILALAKAFPQ
S
//
