ID G4RMU3_THETK Unreviewed; 311 AA.
AC G4RMU3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=pyruvate synthase {ECO:0000256|ARBA:ARBA00012822};
DE EC=1.2.7.1 {ECO:0000256|ARBA:ARBA00012822};
GN Name=oorCD {ECO:0000313|EMBL:CCC80887.1};
GN OrderedLocusNames=TTX_0208 {ECO:0000313|EMBL:CCC80887.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC80887.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC80887.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
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; FN869859; CCC80887.1; -; Genomic_DNA.
DR RefSeq; WP_014126144.1; NC_016070.1.
DR AlphaFoldDB; G4RMU3; -.
DR STRING; 768679.TTX_0208; -.
DR PaxDb; 768679-TTX_0208; -.
DR GeneID; 11263220; -.
DR KEGG; ttn:TTX_0208; -.
DR PATRIC; fig|768679.9.peg.217; -.
DR eggNOG; arCOG01604; Archaea.
DR HOGENOM; CLU_060916_0_0_2; -.
DR OrthoDB; 372091at2157; -.
DR Proteomes; UP000002654; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:RHEA.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR011894; PorC_KorC.
DR InterPro; IPR011898; PorD_KorD.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR NCBIfam; TIGR02175; PorC_KorC; 1.
DR NCBIfam; TIGR02179; PorD_KorD; 1.
DR PANTHER; PTHR43366; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR PANTHER; PTHR43366:SF1; PYRUVATE SYNTHASE SUBUNIT PORC; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCC80887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654}.
FT DOMAIN 239..269
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 281..310
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 311 AA; 33674 MW; 5CFFA3FDA788C209 CRC64;
MRIDTVWIGR GGQGIVTAVY IVAHASIADG FYALANPEFG AERRGAPVKA FLRISDTFED
APEPIKTPDV AVILDDKLID PMRVVIDAVK PGGYVLVSSG KDPEKVAELI GRKDVNIAVV
DGIGIALKHV KLAVPNGPMV GVFARVMGFP KLQSIKEAIE SQLGKAVEQN FAAAEEAYKT
AVIIPATEQG TAKAAVEIPT TSAFLTGDYE LVGWDKIPEG GLTYPGSSLR YKTGSWRVEK
PIIDHSKCIM CRKCWMFCPD DAVLEVWRET KLPSGRVVRV KAIDFSYEYC KGCGICADVC
PTGAIQMVRE I
//
