ID Q8ZTF4_PYRAE Unreviewed; 183 AA.
AC Q8ZTF4;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=pyruvate synthase {ECO:0000256|ARBA:ARBA00012822};
DE EC=1.2.7.1 {ECO:0000256|ARBA:ARBA00012822};
GN OrderedLocusNames=PAE3279 {ECO:0000313|EMBL:AAL64807.1};
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL64807.1, ECO:0000313|Proteomes:UP000002439};
RN [1] {ECO:0000313|EMBL:AAL64807.1, ECO:0000313|Proteomes:UP000002439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC IM2 {ECO:0000313|Proteomes:UP000002439};
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA
CC + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:12765,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=1.2.7.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001135};
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DR EMBL; AE009441; AAL64807.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZTF4; -.
DR STRING; 178306.PAE3279; -.
DR EnsemblBacteria; AAL64807; AAL64807; PAE3279.
DR KEGG; pai:PAE3279; -.
DR PATRIC; fig|178306.9.peg.2469; -.
DR eggNOG; arCOG01603; Archaea.
DR HOGENOM; CLU_087284_2_0_2; -.
DR InParanoid; Q8ZTF4; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR011894; PorC_KorC.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR NCBIfam; TIGR02175; PorC_KorC; 1.
DR PANTHER; PTHR43366; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR PANTHER; PTHR43366:SF1; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002439};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 119..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..174
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
SQ SEQUENCE 183 AA; 19737 MW; 56A96BDD09365480 CRC64;
MSKLLVYEVI FLGRGGQGAV TAAQLLAYAA ALEGKKAQAL PEFGAERRGA IVRAYLRIGE
ALLHSSIKRA DYVVVLDGRI IEQIDVRQYG KPGAVYIVNT KTQADWYVPI DATSIALKYG
LVVAGWTVVN LIMAAAFAAV SGLISLESII KAVPEYVPRK YVDANVKAVI EGYEIAKRLV
KVG
//
