ID M1J4X0_9CREN Unreviewed; 296 AA.
AC M1J4X0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=SacRon12I_11225 {ECO:0000313|EMBL:AGE74459.1};
OS Sulfolobus acidocaldarius Ron12/I.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1028567 {ECO:0000313|Proteomes:UP000011280};
RN [1] {ECO:0000313|EMBL:AGE74459.1, ECO:0000313|Proteomes:UP000011280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ron12/I {ECO:0000313|EMBL:AGE74459.1,
RC ECO:0000313|Proteomes:UP000011280};
RX PubMed=22418622; DOI=10.1038/ismej.2012.20;
RA Mao D., Grogan D.;
RT "Genomic evidence of rapid, global-scale gene flow in a Sulfolobus
RT species.";
RL ISME J. 6:1613-1616(2012).
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; CP002818; AGE74459.1; -; Genomic_DNA.
DR RefSeq; WP_011279041.1; NC_020247.1.
DR AlphaFoldDB; M1J4X0; -.
DR GeneID; 78440240; -.
DR KEGG; sacr:SacRon12I_11225; -.
DR PATRIC; fig|1028567.7.peg.2253; -.
DR HOGENOM; CLU_058423_0_0_2; -.
DR Proteomes; UP000011280; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:AGE74459.1}.
FT DOMAIN 49..204
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 296 AA; 32512 MW; 6562A9C7CBCEB5CF CRC64;
MTLGLREILN KHNSLISGTA ACPGCPENMA MRMLGMGLGK DTVVVVVAGC SSIIQGNAPY
NSYNLPVVNI AFAAGPAAAS GLARAYKQKG KDVNVVVWAG DGGTADIGFA SLSGAAERNE
DIIYVCVDNE AYMNSGGQRS GSTPLGAITS TTPEGKKENK KNLPFLMVSH NVPYVATASV
GYPHDYIQKL KRAKEIDGFR YIHVLTPDPY GWLFDPSRTA EIAKLAVQTC YWPLFEYYNG
KITVSQECLH CLDKRTRRPI KDFLSVQGRF KRVKEDDIAK LEKYIDDMWE KIKELM
//
