ID A0A348B6E2_9CREN Unreviewed; 400 AA.
AC A0A348B6E2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=GCM10007116_14500 {ECO:0000313|EMBL:GGT98026.1},
GN HS1genome_2133 {ECO:0000313|EMBL:BBD73744.1};
OS Sulfodiicoccus acidiphilus.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfodiicoccus.
OX NCBI_TaxID=1670455 {ECO:0000313|EMBL:BBD73744.1, ECO:0000313|Proteomes:UP000276741};
RN [1] {ECO:0000313|Proteomes:UP000276741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-1 {ECO:0000313|Proteomes:UP000276741};
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of Sulfodiicoccus acidiphilus strain HS-1.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBD73744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HS-1 {ECO:0000313|EMBL:BBD73744.1};
RX PubMed=31331368;
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of the Sulfodiicoccus acidiphilus strain HS-1T,
RT the first crenarchaeon that lacks polB3, isolated from an acidic hot spring
RT in Ohwaku-dani, Hakone, Japan.";
RL BMC Res. Notes 12:444-444(2019).
RN [3] {ECO:0000313|EMBL:GGT98026.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGT98026.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [4] {ECO:0000313|EMBL:GGT98026.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGT98026.1};
RA Sun Q., Ohkuma M.;
RL Submitted (SEP-2020) 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; AP018553; BBD73744.1; -; Genomic_DNA.
DR EMBL; BMQS01000012; GGT98026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348B6E2; -.
DR KEGG; sacd:HS1genome_2133; -.
DR Proteomes; UP000276741; Chromosome.
DR Proteomes; UP000616143; Unassembled WGS sequence.
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 CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR32154:SF30; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:BBD73744.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000276741}.
FT DOMAIN 14..236
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 262..357
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 400 AA; 44266 MW; 34670C3DCDE46479 CRC64;
MRKVMSGNEA VARAVKLAKV GVVSIYPITP QTTIIEKLSE MRAEGELSAD IIRVESEHSA
MAGAFGAASA GVRSFTATAS QGLLYMHEMV WWVSGARIPL VMVVATRAVG APWNIWNENT
DFTQLRDAGW VMGFAMNPQE AMDMTIQAFR VSEDSRVFLP AMVGMDGFIL SHTKVPVNVP
TEESVDSFLP LRNQPYVLDP EDPVGMGNMF QPQDYMKLRH SMEQALQSAE EVIREVGRDY
NSKVNSEVNY STLNVTYRVE DADYVVVAMG AWSGDVMEAV DSLREKGISV GLLRLRYLRP
WSSREVREAL KGRKVLVLDR STSLGRGGPL FMEVASTVRG EVEALWGAVS GLGGVSVGKG
EIEELVTEFV EGTKSETEKQ LWFYPGKVRK VELRTPRDVE
//
