GenomeNet

Database: UniProt
Entry: A0A1W6K3Z7_9CREN
LinkDB: A0A1W6K3Z7_9CREN
Original site: A0A1W6K3Z7_9CREN 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system