ID   PORA_METTM              Reviewed;         383 AA.
AC   P80900; D9PUM2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Pyruvate synthase subunit PorA;
DE            EC=1.2.7.1;
DE   AltName: Full=Pyruvate oxidoreductase alpha chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit alpha;
GN   Name=porA; OrderedLocusNames=MTBMA_c03140;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; 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 2-27, 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=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   -!- 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; ADL57920.1; -; Genomic_DNA.
DR   RefSeq; WP_013295147.1; NC_014408.1.
DR   AlphaFoldDB; P80900; -.
DR   SMR; P80900; -.
DR   STRING; 79929.MTBMA_c03140; -.
DR   EnsemblBacteria; ADL57920; ADL57920; MTBMA_c03140.
DR   GeneID; 9704020; -.
DR   KEGG; mmg:MTBMA_c03140; -.
DR   PATRIC; fig|79929.8.peg.308; -.
DR   HOGENOM; CLU_002569_5_0_2; -.
DR   OMA; WNDQQDS; -.
DR   OrthoDB; 29908at2157; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9108258"
FT   CHAIN           2..383
FT                   /note="Pyruvate synthase subunit PorA"
FT                   /id="PRO_0000099898"
SQ   SEQUENCE   383 AA;  42435 MW;  A573D682BA859EBE CRC64;
     MVLKVISANQ AVAEAAKLAK PKVIPVYPIT PQTSISEYLA KYVADGELDA EYIRVESEHS
     AMSACVGASG AGVRVFTATS SQGLALMHEI VYAAAGLRNP IVMANANRAL SAPLSIWNDQ
     QDSIAERDSG WMQIYAESGQ EALDSVLLSY RVSEDRDVLL PSMVCLDGFI LTHTVEPVDI
     PSQDEVDTFL PEFQPQAVLD PDEPMSLGTF TDPNYYMEAR YEVERAMERS RKVIAKACQE
     FSEMFRREYG FVEDYRCEDA EIILVAMGSV CSTLREVIDD MRDEGKPVGL LKVRIHRPFP
     AEEIKKAVSN AHKIAVLDKN ITFSVGGALH TELKALLPDK EVYGFIVGLG GRDITPEHIM
     EIVRKTENPE RTVSWIGLKE ESQ