ID A0A1W6K2D1_9CREN Unreviewed; 493 AA.
AC A0A1W6K2D1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=B6F84_12030 {ECO:0000313|EMBL:ARM76669.1};
OS Acidianus manzaensis.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=282676 {ECO:0000313|EMBL:ARM76669.1, ECO:0000313|Proteomes:UP000193404};
RN [1] {ECO:0000313|EMBL:ARM76669.1, ECO:0000313|Proteomes:UP000193404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN-25 {ECO:0000313|EMBL:ARM76669.1,
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 -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP020477; ARM76669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6K2D1; -.
DR STRING; 282676.B6F84_12030; -.
DR KEGG; aman:B6F84_12030; -.
DR OrthoDB; 6837at2157; -.
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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..101
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..311
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 375..475
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 493 AA; 55668 MW; A0107DC705E7C387 CRC64;
MLGDKIFELL KQFSDRVYGN PGTTELSFIK YLPSDFKYYL ALQDGVAVGM AEGYYLASNK
LAIANLHAAP GLSNALGFIY TALTDRVPLL IIGGQQTSSY LTDEPRLYGD LSNISKPLVK
ASFEAKNTYE AIRYLNRAIK LALTPPYGPT FVSIPEDLES KDIKYNIDPF YHKVNLCCNE
DDIKEIMEIA NSGNVAIISG YEIDAFDAFN EITSFAEKLN SPVYAEPFAS RPPFISSHKL
FAGDLPRRSS EINKVLDNYD VILIIGGSVN NVLFPDEELL GSKKVIEVTY DWIEASKRPW
RTLVCNPKDF LVKAIKYAKP HYGEIKKVVY PRNDKVEEIL KTLYPNLRNY TVFDEVPSYR
EIVRNILGYK KGSLYSNRAG FIGWAIPASF GYSSYGKKSL AIVGDGSFNY SFQALWSASK
YGGKMKVLVI NNQGYNSLRH WNNNINYELL SPNTSPWKLA SSYNFEGKEF DDHKKAIDWL
MSDDTQKLAE IRL
//
