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Database: UniProt
Entry: Q2RMD6
LinkDB: Q2RMD6
Original site: Q2RMD6 
ID   PFOR_MOOTA              Reviewed;        1171 AA.
AC   Q2RMD6;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   13-FEB-2019, entry version 102.
DE   RecName: Full=Pyruvate:ferredoxin oxidoreductase {ECO:0000303|PubMed:9214293};
DE            Short=PFOR {ECO:0000303|PubMed:9214293};
DE            EC=1.2.7.1 {ECO:0000269|PubMed:10878009, ECO:0000305|PubMed:9214293};
DE   AltName: Full=Pyruvate synthase {ECO:0000303|PubMed:10878009};
GN   OrderedLocusNames=Moth_0064 {ECO:0000312|EMBL:ABC18403.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f.
RT   Clostridium thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   REACTION MECHANISM.
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=9214293; DOI=10.1021/bi970403k;
RA   Menon S., Ragsdale S.W.;
RT   "Mechanism of the Clostridium thermoaceticum pyruvate:ferredoxin
RT   oxidoreductase: evidence for the common catalytic intermediacy of the
RT   hydroxyethylthiamine pyropyrosphate radical.";
RL   Biochemistry 36:8484-8494(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   IDENTIFICATION OF PHYSIOLOGICAL ELECTRON CARRIER FOR THE REACTIONS.
RX   PubMed=10878009; DOI=10.1074/jbc.M003291200;
RA   Furdui C., Ragsdale S.W.;
RT   "The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis
RT   during autotrophic growth by the Wood-Ljungdahl pathway.";
RL   J. Biol. Chem. 275:28494-28499(2000).
RN   [4] {ECO:0000244|PDB:6CIN, ECO:0000244|PDB:6CIO, ECO:0000244|PDB:6CIP}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEXES WITH [4FE-4S]
RP   CLUSTERS; THIAMINE PYROPHOSPHATE; LACTYL-TPP AND ACETYL-TPP
RP   INTERMEDIATES; MAGNESIUM AND COA, FUNCTION, COFACTOR, SUBUNIT, AND
RP   REACTION MECHANISM.
RX   PubMed=29581263; DOI=10.1073/pnas.1722329115;
RA   Chen P.Y.-T., Aman H., Can M., Ragsdale S.W., Drennan C.L.;
RT   "Binding site for coenzyme A revealed in the structure of
RT   pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:3846-3851(2018).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of pyruvate to
CC       acetyl-CoA and carbon dioxide. The two electrons that are
CC       generated as a result of pyruvate decarboxylation are used in the
CC       reduction of low potential ferredoxins, which provide reducing
CC       equivalents for central metabolism. Also catalyzes the reverse
CC       reaction, i.e. the synthesis of pyruvate from acetyl-CoA and
CC       carbon dioxide. Appears to function physiologically in both
CC       directions (PubMed:10878009). The oxidation of pyruvate by PFOR is
CC       required to connect glycolysis and the Wood-Ljungdahl pathway of
CC       reductive acetogenesis. The conversion of acetyl-CoA to pyruvate
CC       links the Wood-Ljungdahl pathway of autotrophic CO2 fixation to
CC       the reductive tricarboxylic acid cycle (PubMed:10878009,
CC       PubMed:29581263). Can use methyl viologen as electron carrier in
CC       vitro (PubMed:9214293, PubMed:29581263).
CC       {ECO:0000269|PubMed:10878009, ECO:0000269|PubMed:29581263,
CC       ECO:0000269|PubMed:9214293, ECO:0000305|PubMed:10878009,
CC       ECO:0000305|PubMed:29581263}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate =
CC         acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:12765, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=1.2.7.1;
CC         Evidence={ECO:0000269|PubMed:10878009,
CC         ECO:0000305|PubMed:9214293};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12766;
CC         Evidence={ECO:0000269|PubMed:10878009};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12767;
CC         Evidence={ECO:0000269|PubMed:10878009};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:29581263};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit.
CC       {ECO:0000269|PubMed:29581263};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:29581263};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000269|PubMed:29581263};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:29581263};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000269|PubMed:29581263};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9 uM for acetyl-CoA {ECO:0000269|PubMed:10878009};
CC         KM=2.0 mM for CO2 {ECO:0000269|PubMed:10878009};
CC         KM=0.30 mM for pyruvate {ECO:0000269|PubMed:10878009};
CC         KM=0.32 uM for oxidized ferredoxin
CC         {ECO:0000269|PubMed:10878009};
CC         KM=0.27 uM for reduced ferredoxin {ECO:0000269|PubMed:10878009};
CC         KM=9.4 uM for oxidized rubredoxin {ECO:0000269|PubMed:10878009};
CC         KM=1.1 mM for methyl viologen (in the oxidative decarboxylation
CC         of pyruvate) {ECO:0000269|PubMed:29581263};
CC         Vmax=1.6 umol/min/mg enzyme for the synthesis of pyruvate from
CC         acetyl-CoA and CO2 with methyl viologen as electron donor
CC         {ECO:0000269|PubMed:10878009};
CC         Vmax=1.0 umol/min/mg enzyme for the synthesis of pyruvate with
CC         reduced ferredoxin as electron donor
CC         {ECO:0000269|PubMed:10878009};
CC         Vmax=14.2 umol/min/mg enzyme for the oxidative decarboxylation
CC         of pyruvate with methyl viologen as electron acceptor
CC         {ECO:0000269|PubMed:10878009};
CC         Vmax=14.8 umol/min/mg enzyme for the oxidative decarboxylation
CC         of pyruvate with oxidized ferredoxin as electron acceptor
CC         {ECO:0000269|PubMed:10878009};
CC         Vmax=9.9 umol/min/mg enzyme for the oxidative decarboxylation of
CC         pyruvate with oxidized rubredoxin as electron acceptor
CC         {ECO:0000269|PubMed:10878009};
CC         Note=kcat is 3.2 sec(-1) for the synthesis of pyruvate from
CC         acetyl-CoA and CO2 with methyl viologen as electron donor
CC         (PubMed:10878009). kcat is 2.0 sec(-1) for the synthesis of
CC         pyruvate from acetyl-CoA and CO2 with reduced ferredoxin as
CC         electron donor (PubMed:10878009). kcat is 28 sec(-1) for the
CC         oxidative decarboxylation of pyruvate with methyl viologen as
CC         electron acceptor (PubMed:10878009). kcat is 33 sec(-1) for the
CC         oxidative decarboxylation of pyruvate with methyl viologen as
CC         electron acceptor (PubMed:29581263). kcat is 29.6 sec(-1) for
CC         the oxidative decarboxylation of pyruvate with oxidized
CC         ferredoxin as electron acceptor (PubMed:10878009). kcat is 19.8
CC         sec(-1) for the oxidative decarboxylation of pyruvate with
CC         oxidized rubredoxin as electron acceptor (PubMed:10878009).
CC         {ECO:0000269|PubMed:10878009, ECO:0000269|PubMed:29581263};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29581263}.
CC   -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC       oxidoreductase family. {ECO:0000305}.
DR   EMBL; CP000232; ABC18403.1; -; Genomic_DNA.
DR   RefSeq; WP_011391612.1; NC_007644.1.
DR   RefSeq; YP_428946.1; NC_007644.1.
DR   PDB; 6CIN; X-ray; 2.60 A; A/B/C/D/E/F=1-1171.
DR   PDB; 6CIO; X-ray; 3.00 A; A/B/C/D/E/F=1-1171.
DR   PDB; 6CIP; X-ray; 3.19 A; A/B/C/D/E/F=1-1171.
DR   PDB; 6CIQ; X-ray; 3.30 A; A/B/C=1-1171.
DR   PDBsum; 6CIN; -.
DR   PDBsum; 6CIO; -.
DR   PDBsum; 6CIP; -.
DR   PDBsum; 6CIQ; -.
DR   ProteinModelPortal; Q2RMD6; -.
DR   SMR; Q2RMD6; -.
DR   STRING; 264732.Moth_0064; -.
DR   EnsemblBacteria; ABC18403; ABC18403; Moth_0064.
DR   GeneID; 3830814; -.
DR   KEGG; mta:Moth_0064; -.
DR   PATRIC; fig|264732.11.peg.68; -.
DR   eggNOG; ENOG4105D95; Bacteria.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   HOGENOM; HOG000266425; -.
DR   KO; K03737; -.
DR   OMA; NTVMQVC; -.
DR   OrthoDB; POG091H02IV; -.
DR   BioCyc; MTHE264732:G1G5J-72-MONOMER; -.
DR   Proteomes; UP000007053; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.920.10; -; 1.
DR   Gene3D; 4.10.780.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR   InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   Pfam; PF10371; EKR; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PIRSF; PIRSF000159; NifJ; 1.
DR   SMART; SM00890; EKR; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   SUPFAM; SSF53323; SSF53323; 1.
DR   TIGRFAMs; TIGR02176; pyruv_ox_red; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Magnesium; Metal-binding; Oxidoreductase; Pyruvate;
KW   Reference proteome; Transport.
FT   CHAIN         1   1171       Pyruvate:ferredoxin oxidoreductase.
FT                                /FTId=PRO_0000446263.
FT   DOMAIN      677    706       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      733    764       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   REGION      424    428       CoA binding.
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIQ}.
FT   REGION      967    969       Thiamine pyrophosphate binding.
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   REGION      995   1000       Thiamine pyrophosphate binding.
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       686    686       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       689    689       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       692    692       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       696    696       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       742    742       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       745    745       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       748    748       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       752    752       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       809    809       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       812    812       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       837    837       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       967    967       Magnesium. {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       995    995       Magnesium. {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL       997    997       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   METAL      1075   1075       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   BINDING      29     29       Pyruvate. {ECO:0000305|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIO}.
FT   BINDING     112    112       Pyruvate. {ECO:0000305|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIO}.
FT   BINDING     456    456       CoA; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIQ}.
FT   BINDING     556    556       CoA. {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIQ}.
FT   BINDING     598    598       CoA. {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIQ}.
FT   BINDING     814    814       Thiamine pyrophosphate.
FT                                {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIO}.
FT   BINDING     837    837       Thiamine pyrophosphate; via amide
FT                                nitrogen. {ECO:0000269|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIN}.
FT   BINDING    1000   1000       Pyruvate. {ECO:0000305|PubMed:29581263,
FT                                ECO:0000312|PDB:6CIO}.
SQ   SEQUENCE   1171 AA;  127277 MW;  3F171E506F8D9B6E CRC64;
     MPKQTLDGNT AAAHVAYAMS EVATIYPITP SSPMAEIADE WAAHGRKNIF GKTLQVAEMQ
     SEAGAAGAVH GSLAAGALTT TFTASQGLLL MIPNMYKIAG ELLPCVFHVA ARALSTHALS
     IFGDHADVMA ARQTGFAMLS SASVQEVMDL ALVAHLATLK ARVPFVHFFD GFRTSHEVQK
     IDVIEYEDMA KLVDWDAIRA FRQRALNPEH PHQRGTAQNP DIYFQSREAA NPYYLATPGI
     VAQVMEQVAG LTGRHYHLFD YAGAPDAERV IVSMGSSCEV IEETVNYLVE KGEKVGLIKV
     RLFRPFSAEH FLKVLPASVK RIAVLDRTKE PGSLGEPLYE DVQTVLAEHG KNILVVGGRY
     GLGSKEFNPS MVKAVFDNLA ATTPKNKFTV GITDDVTHTS LEIKEHIDTS PKGTFRCKFF
     GLGSDGTVGA NKNSIKIIGD HTDMYAQGYF VYDSKKSGGV TISHLRFGKQ PIQSAYLIDQ
     ADLIACHNPS YVGRYNLLEG IKPGGIFLLN STWSAEEMDS RLPADMKRTI ATKKLKFYNI
     DAVKIAQEIG LGSRINVIMQ TAFFKIANVI PVDEAIKYIK DSIVKTYGKK GDKILNMNFA
     AVDRALEALE EIKYPASWAD AVDEAAATVT EEPEFIQKVL RPINALKGDE LPVSTFTPDG
     VFPVGTTKYE KRGIAVNIPQ WQPENCIQCN QCSLVCPHAA IRPYLAKPAD LAGAPETFVT
     KDAIGKEAAG LKFRIQVSPL DCTGCGNCAD VCPAKVKALT MVPLEEVTAV EEANYNFAEQ
     LPEVKVNFNP ATVKGSQFRQ PLLEFSGACA GCGETPYVKL VTQLFGDRMI IANATGCSSI
     WGGSAPACPY TVNRQGHGPA WASSLFEDNA EFGYGMALAV AKRQDELATA ISKALEAPVS
     AAFKAACEGW LAGKDDADRS REYGDRIKAL LPGEISQASG EVKDLLLDID RQKDYLTKKS
     IWIIGGDGWA YDIGYGGLDH VLASGANVNV LVLDTEVYSN TGGQSSKATQ TGAVARFAAG
     GKFTKKKDLG LMAMSYGYVY VASVAMGASH SQLMKALIEA EKYDGPSLII AYAPCINHGI
     NMTYSQREAK KAVEAGYWPL YRYNPQLAQE GKNPFILDYK TPTASFRDFL MGEIRYTSLK
     KQFPEKAEQL FAKAEADAKA RLEQYKKLAE G
//
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