ID A3MTX6_PYRCJ Unreviewed; 392 AA.
AC A3MTX6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=Pcal_0667 {ECO:0000313|EMBL:ABO08093.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359 {ECO:0000313|EMBL:ABO08093.1, ECO:0000313|Proteomes:UP000001431};
RN [1] {ECO:0000313|EMBL:ABO08093.1, 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 -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000256|ARBA:ARBA00011631}.
CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain. {ECO:0000256|ARBA:ARBA00011595}.
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DR EMBL; CP000561; ABO08093.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MTX6; -.
DR STRING; 410359.Pcal_0667; -.
DR KEGG; pcl:Pcal_0667; -.
DR eggNOG; arCOG01608; Archaea.
DR HOGENOM; CLU_002569_5_0_2; -.
DR OrthoDB; 372068at2157; -.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate 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; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; 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 Oxidoreductase {ECO:0000313|EMBL:ABO08093.1};
KW Pyruvate {ECO:0000313|EMBL:ABO08093.1}.
FT DOMAIN 21..241
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 264..370
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 392 AA; 43020 MW; CF219CEB411D8688 CRC64;
MQVEKTKLRE ALTGNYAAAY AVKAVDVDVI AVYPITPQTT IVEKLSEFVA NGELNAEIIH
VESEHSALSA VVGASAAGAR VFTATSSQGL ELAHEVLHIA SGLRLPIVMA VPARAISAPI
SIHNDYGDVM NARDTGWVIY IAATAQEVYD TIIQAYRVAE SVFLPVMVAY DGFLMSHTVE
PVELNDEDEV RKFVPRALRP YTLNPKRPVT LGALASPDWY YEFKYQQVEA MREAYKVAKD
VDAQYKAKFG RGYGVVETYR MEDADYAIVA YGGAAYGNAR AAADLARERG IAAGVVRVRL
YRPFPTADVL RALSGVKAFA VVDRAIMFGS PAEGPLYKDI ATAMYMHGVD KPAVNIIHGI
GQRAMYVEDF YKVYTMLREG PKREVVFMGV RV
//
