ID A0A0F2L4J0_9CREN Unreviewed; 314 AA.
AC A0A0F2L4J0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=TU36_02415 {ECO:0000313|EMBL:KJR72383.1};
OS Vulcanisaeta sp. AZ3.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1609231 {ECO:0000313|EMBL:KJR72383.1, ECO:0000313|Proteomes:UP000054362};
RN [1] {ECO:0000313|EMBL:KJR72383.1, ECO:0000313|Proteomes:UP000054362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000256|ARBA:ARBA00011631}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR72383.1}.
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DR EMBL; JZWU01000049; KJR72383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2L4J0; -.
DR PATRIC; fig|1609231.3.peg.1608; -.
DR Proteomes; UP000054362; Unassembled WGS sequence.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03375; TPP_OGFOR; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR011896; OFOB.
DR InterPro; IPR032686; PFO_beta_C.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; NF041171; Oxoac_fdxbeta_Archa; 1.
DR NCBIfam; TIGR02177; PorB_KorB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR PANTHER; PTHR48084:SF2; PYRUVATE FERREDOXIN_FLAVODOXIN OXIDOREDUCTASE, BETA SUBUNIT; 1.
DR Pfam; PF12367; PFO_beta_C; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 51..198
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 202..273
FT /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12367"
SQ SEQUENCE 314 AA; 34797 MW; AC47544407F37328 CRC64;
MAHKLTINDY KTDVWIDWCP GCGNYGILSA MYQAFAELQL DPTKTVVVGG IGCSGKTPHF
INVTGVHTLH GRSLPYAEGI KLSNPDLTVI ANVGDGDLLG IGAAHFVALG RRNVDLVVIM
HDNTVYALTK GQASPTLARN LQPKALPKPN LQDAVNPIGL AIASGYTFIA RGYAARVQHL
KELIKKAIEH KGSAFIDVLQ PCVTYDNIHT YDYYNKRVYD INEEGWDPIV HSPEELPQKV
SQALAKSYEG DGRIPIGIFL INPYVPTFEE RYSGRLPSYL KVPPAREVIE VNSKPVITME
KFKEIFSKYI IEFK
//
