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Database: UniProt
Entry: A6M1E8_CLOB8
LinkDB: A6M1E8_CLOB8
Original site: A6M1E8_CLOB8 
ID   A6M1E8_CLOB8            Unreviewed;      1169 AA.
AC   A6M1E8;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=Pyruvate:ferredoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.1 {ECO:0000256|PIRNR:PIRNR000159};
DE   AltName: Full=Pyruvate synthase {ECO:0000256|PIRNR:PIRNR000159};
GN   OrderedLocusNames=Cbei_4318 {ECO:0000313|EMBL:ABR36428.1};
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR36428.1, ECO:0000313|Proteomes:UP000000565};
RN   [1] {ECO:0000313|EMBL:ABR36428.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR36428.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=21962126; DOI=10.1186/1471-2164-12-479;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Single-nucleotide resolution analysis of the transcriptome structure of
RT   Clostridium beijerinckii NCIMB 8052 using RNA-Seq.";
RL   BMC Genomics 12:479-479(2011).
RN   [3] {ECO:0000313|EMBL:ABR36428.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=22433311; DOI=10.1186/1471-2164-13-102;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Genome-wide dynamic transcriptional profiling in clostridium beijerinckii
RT   NCIMB 8052 using single-nucleotide resolution RNA-Seq.";
RL   BMC Genomics 13:102-102(2012).
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         Evidence={ECO:0000256|PIRNR:PIRNR000159};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000159-50};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000159-50};
CC   -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009032,
CC       ECO:0000256|PIRNR:PIRNR000159}.
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DR   EMBL; CP000721; ABR36428.1; -; Genomic_DNA.
DR   RefSeq; WP_012060475.1; NC_009617.1.
DR   AlphaFoldDB; A6M1E8; -.
DR   KEGG; cbe:Cbei_4318; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1013; Bacteria.
DR   eggNOG; COG1014; Bacteria.
DR   HOGENOM; CLU_002569_0_0_9; -.
DR   OMA; NTVMQVC; -.
DR   Proteomes; UP000000565; 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   CDD; cd03377; TPP_PFOR_PNO; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   Gene3D; 4.10.780.10; Pyruvate-flavodoxin oxidoreductase, EKR domain; 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_TPP-bd.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR02176; pyruv_ox_red; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF10371; EKR; 1.
DR   Pfam; PF12838; Fer4_7; 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; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000159-50};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|PIRNR:PIRNR000159};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000159-50};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000159-
KW   50};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000159-50};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000159}; Pyruvate {ECO:0000313|EMBL:ABR36428.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN          680..709
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          737..768
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         30
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         63
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         113
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         689
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         692
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         695
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         699
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         746
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         749
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         752
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         756
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         813
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         816
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         818
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         841
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         841
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         961..964
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         990..995
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         1070
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   SITE            30
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            63
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            113
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            995
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ   SEQUENCE   1169 AA;  127393 MW;  3EF89A47373DDDCA CRC64;
     MRKMKTMDGN TAAAHISYAF TEVSAIFPIT PSSPMAEHVD EWVAQGRKNI FGQPVKVMEM
     QSEAGAAGAV HGSLQAGALT TTYTASQGLL LMIPNMYKIS GEMLPGVFHV SARALATSAL
     NIFGDHQDVM AARQTGFAML AEGSVQEVMD LAAVAHLTAI KTRIPFLNFF DGFRTSHEVQ
     KIEVLEYDEL ASLLDWDSVK AFRERALNPN HPVTRGTAQN ADIYFQERES VNKFYNELPE
     TVENYMAEIT KLTGREYHCF DYYGAPDADR VIIAMGSATD VCEETIDYLN ANGQKVGVIK
     VRLFRPFSNE RLLAAIPKTV KKIAVLDRTK EPGSTGEPLY LDVRNAFYGQ ANAPLIVGGR
     FGLGSKDPNP GHIAAVYANL AQDAPKNGFT IGIVDDVTNT SLEVTEDIDA TPEGTTSCKF
     WGLGSDGTVG ANKSAIKIIG DNTDMYAQAY FFYDSKKSGG ITVSHLRFGK KAIKSPYLIN
     KADFVSCSNQ SYIHKYNVLE GLKPGSTFLL NTIWSPEDLE EKLPASYKRF LANNNIKFYT
     INAVGIAQEI GLGGRINMIM QSAFFKLANI IPVEDAIKHL KDSVVTSYGK KGEKVVNMNN
     AAIDKGVESI VAIDIPEAWK TVADEAPVEI KHATKFVKDI VIPMNRQEGD QLPVSAFAGM
     EDGTFENGTA AFEKRGIAVN VPEWDKDKCI QCNQCSMVCP HASIRPFLLT EAEKNAAPSA
     NKAVAAKGLK TEEPLFYTMG VTPLDCSGCG NCAQVCPAPG KALVMKPQES QHDQIEAWDY
     LTHDISVKKN PMNKKTVKGS QFEQPLLEFS GACAGCGETP YVKAITQLVG DRMMVANATG
     CTSIWGGSAP STPYTKNKNG HGPAWANSLF EDNAEYGLGM FLGVKAIRER IAEKAEAAIA
     ANDPAKAELQ EWLDNVNEGE GTRERADKLT AALEASNTEL AKEILAEKDY FVKRSQWIFG
     GDGWAYDIGY GGVDHVLASG EDVNILVVDT EVYSNTGGQS SKATPTAAIA KFAASGKKTK
     KKDLGMMAMS YGYVYVAQIN MGADKNQVMK AIAEAEAYKG PSLIIAYAPC INHGLRIGMG
     NSQEEAKRAT ACGYWQMYRF NPELKDAGKN PFSLDSKEPT ADFKEFLMGE VRYSSLAKAF
     PEQADALFEK TKKDAMERLE GYKKLANQQ
//
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