ID PORB_THEMA Reviewed; 324 AA.
AC Q56317;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 128.
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=TM_0018;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17 AND 20-44.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
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 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X85171; CAA59458.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35112.1; -; Genomic_DNA.
DR PIR; B59427; D72427.
DR RefSeq; NP_227834.1; NC_000853.1.
DR RefSeq; WP_004082462.1; NZ_CP011107.1.
DR AlphaFoldDB; Q56317; -.
DR SMR; Q56317; -.
DR STRING; 243274.TM_0018; -.
DR PaxDb; 243274-THEMA_04710; -.
DR EnsemblBacteria; AAD35112; AAD35112; TM_0018.
DR KEGG; tma:TM0018; -.
DR eggNOG; COG1013; Bacteria.
DR InParanoid; Q56317; -.
DR OrthoDB; 9794954at2; -.
DR BioCyc; MetaCyc:MONOMER-424; -.
DR BRENDA; 1.2.7.1; 6331.
DR Proteomes; UP000008183; 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 CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 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..324
FT /note="Pyruvate synthase subunit PorB"
FT /id="PRO_0000099909"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
SQ SEQUENCE 324 AA; 36385 MW; 2425239D778A6A0E CRC64;
MPVNIKQLAQ EFDKKEIGIT QGHRLCPGCG APITVKFVMM IARHLGYEPV VGLATGCLEV
STSIYPYTAW SVPYIHNAFE NVAATMSGVE TAYKALKNKG KIPEDKKYAF IAFGGDGGTY
DIGLQSLSGM LERGHKVLYV LYDNEGYMNT GNQRSGSTPP GSDTTTAPVG KKLPGKVQLK
KNIVEIVAAH ENVYAATASL SEPMDFFAKV EKALNFDGPS FLAVFSPCVR FWRVNDDKTV
EISKLAVETK YWPLYEVERG VYRVTRKPRQ FKPVEEFLKA QGRFRKLLSR PDAKEIVDEL
QEYVDRRWER LLTLEEVTKD KPIR
//
