ID A3MSC8_PYRCJ Unreviewed; 311 AA.
AC A3MSC8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=Pcal_0107 {ECO:0000313|EMBL:ABO07545.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359 {ECO:0000313|EMBL:ABO07545.1, ECO:0000313|Proteomes:UP000001431};
RN [1] {ECO:0000313|EMBL:ABO07545.1, ECO:0000313|Proteomes:UP000001431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1
RC {ECO:0000313|Proteomes:UP000001431};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) 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}.
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DR EMBL; CP000561; ABO07545.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MSC8; -.
DR STRING; 410359.Pcal_0107; -.
DR KEGG; pcl:Pcal_0107; -.
DR eggNOG; arCOG01599; Archaea.
DR HOGENOM; CLU_048564_0_0_2; -.
DR Proteomes; UP000001431; Chromosome.
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 Pyruvate {ECO:0000313|EMBL:ABO07545.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 52..199
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 203..277
FT /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12367"
SQ SEQUENCE 311 AA; 34976 MW; F4960B082E32A48D CRC64;
MVQTRRTPAD YRWVRPPEWC PGCGHFGVLQ AVYNAFAELD LDPSRVVLVS GIGCSSRLPH
FVKTTSVHAI HGRAIPYAMG IKLANPSLEV VVVGGDGDLM AIGGNHLLHM GRRNIDMTVI
LMDNSVYGLT RGQAGPTLPA GIKVKAIPKA NPQSEINPLL LALTAGFTFI ARGYSYDIKY
TTKLIVEAIR HKGSAFVQIY SPCVTYNNVM TREWYEKRIY KLEEADPTWD PVVHDEKEVD
IKIRKALDKI VERDRLPLGI FYKNELVPTF EERYEAIYDP HYRKLPPAIQ PIEVDGRPVV
DLEKLLADRI L
//
