ID   PORB_PYRFU              Reviewed;         331 AA.
AC   Q51805;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Pyruvate synthase subunit PorB;
DE            EC=1.2.7.1;
DE   AltName: Full=Pyruvate oxidoreductase beta chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit beta;
GN   Name=porB; OrderedLocusNames=PF0965;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=8550425; DOI=10.1128/jb.178.1.248-257.1996;
RA   Kletzin A., Adams M.W.W.;
RT   "Molecular and phylogenetic characterization of pyruvate and 2-
RT   ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and
RT   pyruvate ferredoxin oxidoreductase from Thermotoga maritima.";
RL   J. Bacteriol. 178:248-257(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=8380721; DOI=10.1016/0167-4838(93)90190-3;
RA   Blamey J.M., Adams M.W.W.;
RT   "Purification and characterization of pyruvate ferredoxin oxidoreductase
RT   from the hyperthermophilic archaeon Pyrococcus furiosus.";
RL   Biochim. Biophys. Acta 1161:19-27(1993).
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P94692};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P94692};
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain.
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DR   EMBL; X85250; CAA59506.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81089.1; -; Genomic_DNA.
DR   PIR; T45089; T45089.
DR   RefSeq; WP_011012102.1; NC_018092.1.
DR   AlphaFoldDB; Q51805; -.
DR   SMR; Q51805; -.
DR   STRING; 186497.PF0965; -.
DR   EnsemblBacteria; AAL81089; AAL81089; PF0965.
DR   GeneID; 41712777; -.
DR   KEGG; pfu:PF0965; -.
DR   PATRIC; fig|186497.12.peg.1024; -.
DR   eggNOG; arCOG01601; Archaea.
DR   HOGENOM; CLU_058423_0_0_2; -.
DR   OMA; ATGCMEV; -.
DR   OrthoDB; 29720at2157; -.
DR   PhylomeDB; Q51805; -.
DR   BRENDA; 1.2.7.1; 5243.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8550425"
FT   CHAIN           2..331
FT                   /note="Pyruvate synthase subunit PorB"
FT                   /id="PRO_0000099907"
FT   BINDING         21
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         24
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         59
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         222
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
SQ   SEQUENCE   331 AA;  36261 MW;  1523640D21AB7D12 CRC64;
     MAVRKPPITT REYWAPGHAA CAGCGCATAL RLATKALSEA MEEKYGDPNA FAIAHATGCM
     EVVSAVFPYT AWKAPWIHVA FENAAAVASG IEAAWKKLGR KGKILAIGGD GGTADIGLQA
     LSGMLERWHN VLYLMYDNEA YMNTGIQRSS STPYGAWTTT SPPGKYSVGE DKPKKWVALI
     AAAHQIPYVA TASIGNPLDF VRKIKKAGKI DGPAFVQVLC TCPTGWRSPL EKGVEIARLA
     IETGIWPLFE IENGDIWNIK IQPPGGGAKV YKEGNRVVRI EFKKPIEEYL KLQGRFKHLF
     KRPEAIEELR NQVKAMWKVL GVEAILPRPE E