ID A0A1W6K3Z7_9CREN Unreviewed; 297 AA.
AC A0A1W6K3Z7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=B6F84_13220 {ECO:0000313|EMBL:ARM77205.1};
OS Acidianus manzaensis.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=282676 {ECO:0000313|EMBL:ARM77205.1, ECO:0000313|Proteomes:UP000193404};
RN [1] {ECO:0000313|EMBL:ARM77205.1, ECO:0000313|Proteomes:UP000193404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN-25 {ECO:0000313|EMBL:ARM77205.1,
RC ECO:0000313|Proteomes:UP000193404};
RA Ma Y., Yang Y., Xia J.;
RT "Sulfur activation and transportation mechanism of thermophilic Archaea
RT Acidianus manzaensis YN-25.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation
CC of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-
CC oxobutyrate to form their CoA derivatives.
CC {ECO:0000256|ARBA:ARBA00003908}.
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; CP020477; ARM77205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6K3Z7; -.
DR STRING; 282676.B6F84_13220; -.
DR KEGG; aman:B6F84_13220; -.
DR OrthoDB; 296931at2157; -.
DR Proteomes; UP000193404; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0047553; F:2-oxoglutarate 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 65..202
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 297 AA; 32939 MW; 7488972B9A9391C9 CRC64;
MSLITNPRRI PKLYRGNAAC PGCPIPKELD ILIEELGEKA VLVVPASCTT VIMGDTTGMP
STIPVVHSAF AAASPIASGI VRSLRMKGDN DSIVAVWAGD GGTADIGFSA ISGSAERNED
ILYVCYDNEA YMNTGIQRSS LTPKGAWTTT TPEGKREFKK PMPFIMAEHK IPYVATASVA
YPFDYQNKVK KAKQIKGFRY VHLLSPCPPG WRFDSSLTIE IAKLAVETGI WPLFEIENGE
FRLTSISKTL IDKKNRKPVT EYLKLQGRFS KLNEKEIKEI EDSVDELWEE IKSYIKQ
//