ID   PORB_METTM              Reviewed;         288 AA.
AC   P80901; D9PUM1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   02-SEP-2026, entry version 89.
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=MTBMA_c03130;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanobacteria; Methanobacteriales; Methanobacteriaceae;
OC   Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=9108258; DOI=10.1111/j.1432-1033.1997.00862.x;
RA   Tersteegen A., Linder D., Thauer R.K., Hedderich R.;
RT   "Structures and functions of four anabolic 2-oxoacid oxidoreductases in
RT   Methanobacterium thermoautotrophicum.";
RL   Eur. J. Biochem. 244:862-868(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate + CoA = 2 reduced
CC         [2Fe-2S]-[ferredoxin] + acetyl-CoA + CO2 + H(+);
CC         Xref=Rhea:RHEA:12765, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57287,
CC         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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 10.0. {ECO:0000269|PubMed:9108258};
CC       Temperature dependence:
CC         Optimum temperature is 80 degrees Celsius.
CC         {ECO:0000269|PubMed:9108258};
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain. {ECO:0000269|PubMed:9108258}.
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DR   EMBL; CP001710; ADL57919.1; -; Genomic_DNA.
DR   RefSeq; WP_013295146.1; NC_014408.1.
DR   AlphaFoldDB; P80901; -.
DR   SMR; P80901; -.
DR   STRING; 79929.MTBMA_c03130; -.
DR   PaxDb; 79929-MTBMA_c03130; -.
DR   GeneID; 41326762; -.
DR   GeneID; 9704019; -.
DR   KEGG; mmg:MTBMA_c03130; -.
DR   PATRIC; fig|79929.8.peg.307; -.
DR   HOGENOM; CLU_058423_0_0_2; -.
DR   OrthoDB; 296931at2157; -.
DR   Proteomes; UP000000345; Chromosome.
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; IPR051479; PorB-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; NF008819; PRK11865.1; 1.
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   CHAIN           1..288
FT                   /note="Pyruvate synthase subunit PorB"
FT                   /id="PRO_0000099905"
FT   REGION          137..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         16
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         19
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         44
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         208
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   CONFLICT        6
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="A -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   288 AA;  31623 MW;  550DAA6D2BCB6D04 CRC64;
     MKIPEEEFLA PGHRGCAGCG ATVGVRLALK VLGKNTVAVS STGCLEVITT PYPETAWEIP
     WIHVAFENAA AVASGVERAL RARGRGEVNV VAFAGDGGTA DIGLQSLSGA MERGHNIIYI
     CYDNEAYMNT GIQRSASTPY GASTTTSPHG KESFGEDRPK KNMPLIMAAH GVPYVATASI
     SYPEDFMEKV RKARDIEGPA YIHLHQPCTT GWGFDPSKTV ELGRLAVETG SWILYEIEDG
     DFRVTYRPVQ RKPVEEYLNA QKRFRHLTEE QKAKIQEYVD SVCQELRI
//