GenomeNet

Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: PORA_THEMA G4FGT3_THEMA
LinkDB: PORA_THEMA G4FGT3_THEMA
Original site: PORA_THEMA G4FGT3_THEMA 
ID   PORA_THEMA              Reviewed;         392 AA.
AC   O05651;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   24-JAN-2024, entry version 131.
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=TM_0017;
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 1-43.
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-43, AND CHARACTERIZATION.
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=8305426; DOI=10.1021/bi00170a019;
RA   Blamey J.M., Adams M.W.W.;
RT   "Characterization of an ancestral type of pyruvate ferredoxin
RT   oxidoreductase from the hyperthermophilic bacterium, Thermotoga maritima.";
RL   Biochemistry 33:1000-1007(1994).
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   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD35111.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA59457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; CAA59457.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE000512; AAD35111.1; ALT_INIT; Genomic_DNA.
DR   PIR; D59427; C72427.
DR   RefSeq; NP_227833.1; NC_000853.1.
DR   RefSeq; WP_004082460.1; NZ_CP011107.1.
DR   AlphaFoldDB; O05651; -.
DR   SMR; O05651; -.
DR   STRING; 243274.TM_0017; -.
DR   PaxDb; 243274-THEMA_04715; -.
DR   EnsemblBacteria; AAD35111; AAD35111; TM_0017.
DR   KEGG; tma:TM0017; -.
DR   PATRIC; fig|243274.5.peg.15; -.
DR   eggNOG; COG0674; Bacteria.
DR   InParanoid; O05651; -.
DR   OMA; WNDQQDS; -.
DR   OrthoDB; 9794954at2; -.
DR   BioCyc; MetaCyc:MONOMER-423; -.
DR   BRENDA; 1.2.7.1; 6331.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 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   NCBIfam; NF040682; PorA_Arch; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Reference proteome.
FT   CHAIN           1..392
FT                   /note="Pyruvate synthase subunit PorA"
FT                   /id="PRO_0000099902"
SQ   SEQUENCE   392 AA;  44112 MW;  ACEF0E34C9EC1818 CRC64;
     MERVVERVAV TGAEAVANAM RQIEPDVVAA YPITPQTPIV EYFARFVADG VVRTEMIPVE
     SEHSAMSAVV GAAAAGARAM TATSANGLAL MHEIVYIAAS YRLPIVMPVV NRALSGPINI
     HCDHSDAMAE RDSGWIQLFA ETNQEAYDFT ILAVRLAEHE DVRLPVMVNL DGFILSHGVE
     PVEFYPDELV KKFVGELKPM YPLLDTEHPV TWGPLDLYDY YFEHKRQQIE AMENVKKVFP
     EIAKEFEETF GRKYWFVEPY RMEDAEHVMV ALGSTNSTIK YVVDELREEG YKVGSLKIWM
     FRPFPKEQLQ ELLNGRKSVV VLDRAVSFGA EAPLYEAVKS ALYEVAARPM LGSYVYGLGG
     RDIKPEHIRK AFEDAINGNL IADEQRYLGL RE
//
ID   G4FGT3_THEMA            Unreviewed;       392 AA.
AC   G4FGT3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Pyruvate:ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:AGL48940.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:AGL48940.1};
GN   ORFNames=Tmari_0014 {ECO:0000313|EMBL:AGL48940.1};
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 {ECO:0000313|EMBL:AGL48940.1, ECO:0000313|Proteomes:UP000013901};
RN   [1] {ECO:0000313|EMBL:AGL48940.1, ECO:0000313|Proteomes:UP000013901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC   {ECO:0000313|Proteomes:UP000013901};
RX   PubMed=23637642;
RA   Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA   Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA   Zengler K.;
RT   "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL   PLoS Genet. 9:E1003485-E1003485(2013).
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; CP004077; AGL48940.1; -; Genomic_DNA.
DR   RefSeq; WP_004082460.1; NZ_CP011107.1.
DR   AlphaFoldDB; G4FGT3; -.
DR   SMR; G4FGT3; -.
DR   KEGG; tmm:Tmari_0014; -.
DR   KEGG; tmw:THMA_0013; -.
DR   PATRIC; fig|243274.17.peg.16; -.
DR   OMA; WNDQQDS; -.
DR   Proteomes; UP000013901; 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   Gene3D; 3.40.50.970; -; 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   NCBIfam; NF040682; PorA_Arch; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:AGL48940.1};
KW   Pyruvate {ECO:0000313|EMBL:AGL48940.1}.
FT   DOMAIN          19..243
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          265..368
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   392 AA;  44112 MW;  ACEF0E34C9EC1818 CRC64;
     MERVVERVAV TGAEAVANAM RQIEPDVVAA YPITPQTPIV EYFARFVADG VVRTEMIPVE
     SEHSAMSAVV GAAAAGARAM TATSANGLAL MHEIVYIAAS YRLPIVMPVV NRALSGPINI
     HCDHSDAMAE RDSGWIQLFA ETNQEAYDFT ILAVRLAEHE DVRLPVMVNL DGFILSHGVE
     PVEFYPDELV KKFVGELKPM YPLLDTEHPV TWGPLDLYDY YFEHKRQQIE AMENVKKVFP
     EIAKEFEETF GRKYWFVEPY RMEDAEHVMV ALGSTNSTIK YVVDELREEG YKVGSLKIWM
     FRPFPKEQLQ ELLNGRKSVV VLDRAVSFGA EAPLYEAVKS ALYEVAARPM LGSYVYGLGG
     RDIKPEHIRK AFEDAINGNL IADEQRYLGL RE
//
DBGET integrated database retrieval system