PORB_PYRHO
ID PORB_PYRHO Reviewed; 331 AA.
AC O58417;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
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=PH0685;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29776.1; ALT_INIT; Genomic_DNA.
DR PIR; F71114; F71114.
DR RefSeq; WP_048053193.1; NC_000961.1.
DR AlphaFoldDB; O58417; -.
DR SMR; O58417; -.
DR STRING; 70601.3257093; -.
DR EnsemblBacteria; BAA29776; BAA29776; BAA29776.
DR GeneID; 1443012; -.
DR KEGG; pho:PH0685; -.
DR eggNOG; arCOG01601; Archaea.
DR OMA; ATGCMEV; -.
DR OrthoDB; 29720at2157; -.
DR Proteomes; UP000000752; 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 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..331
FT /note="Pyruvate synthase subunit PorB"
FT /id="PRO_0000099908"
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; 36119 MW; 2E5FDCE5B6791C25 CRC64;
MAVRKPPITT REYWAPGHAA CAGCGCAIAL KLATKAFSEA MEEKYGDPNA FAIAQATGCM
EVVSAVFPYT AWKVPWIHVA FENAAAAASG VEAAWKKLGI KGKILAIGGD GGTADIGLQA
LSGMLERGHN VVYLMYDNEA YMNTGIQRSS STPYGAWTTT SPPGKYSIGE DRPKKWVALI
AAAHQIPYAA TASIGNPFDL VKKVKKAAKV DGPAFIQVHC TCPTGWRTPL EKGVEIARLA
IETGMWPLFE IENGDIWNIK IQPPGGGAKV YKEGGRVVRI EFKKPIEEYL KYQGRFKHLF
KRPEAIEELR NQIKAMWKVL GVEAILPRPE E