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Database: UniProt
Entry: A0A0J1F7Z0_9FIRM
LinkDB: A0A0J1F7Z0_9FIRM
Original site: A0A0J1F7Z0_9FIRM 
ID   A0A0J1F7Z0_9FIRM        Unreviewed;      1168 AA.
AC   A0A0J1F7Z0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   Name=nifJ_3 {ECO:0000313|EMBL:KLU59427.1};
GN   ORFNames=CEB3_c44130 {ECO:0000313|EMBL:KLU59427.1};
OS   Peptococcaceae bacterium CEB3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU59427.1, ECO:0000313|Proteomes:UP000035957};
RN   [1] {ECO:0000313|EMBL:KLU59427.1, ECO:0000313|Proteomes:UP000035957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEB3 {ECO:0000313|EMBL:KLU59427.1,
RC   ECO:0000313|Proteomes:UP000035957};
RA   Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA   Muehling M.;
RT   "Genome sequence of the moderately acidophilic sulfate reducing
RT   Peptococcaceae bacterium strain CEB3.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLU59427.1}.
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DR   EMBL; LDXJ01000063; KLU59427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1F7Z0; -.
DR   STRING; 999898.CEB3_c44130; -.
DR   PATRIC; fig|999898.3.peg.4943; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000035957; Unassembled WGS sequence.
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:0019164; F:pyruvate synthase activity; IEA:RHEA.
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:KLU59427.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035957};
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          734..765
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         31
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         64
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         114
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         743
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         753
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         809
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         812
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         814
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         837
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         837
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            31
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            64
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            114
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   1168 AA;  127519 MW;  5B15746BDC4F111E CRC64;
     MARKMQTMDG NTAAAHTSYA FTDVAAIYPI TPSTPMAEHV DEWSVRGRKN IFGQTVKLVE
     MQSEGGAAGA VHGSLQAGAL TTTYTSSQGL LLMIPNMYKI AGELLPAVFH VSARALGANA
     LAIFGDHQDV MATRQTGFAM LAESSVQQVM DLAAVAHLSA IKGRVPFVNF FDGFRTSHEV
     QKIEVLDYDE LAPLVDKTAL EEFRRKALNP DHPVMKGTVQ NSDIYFQQRE VSNRYYQALP
     EIVENYMAEI NKLTGRDYHL FNYYGAADAD RMIIAMGSVC EAIEETVDYL NARGEKVGVL
     TVHLYRPFSL EHFFKYIPKT VRKIAVLDRT KELGAFAEPL YLDVKAVFSG RDWQPVIVGG
     RCGVGGKDVV PGHIQGIFAN LNQAQPKDHF TVGIVDDVTH TSLPFGEDID PTAAGTTACK
     FWGLGSDGTV GANKSAITII GDHTDMYAQG YFAYDSKKSG GVTISHLRFG KSPIKSPYLI
     NKADFIACHN QSYVDKYNVL EGLKPGGSFL LNCNWTAGEL ENHLPAGMKR YMFKNKIRFY
     TLDAVGIAQK IGLGGRINMI MQAAFFKIAG IIPVEEAVRY LKEAAEKSYG KKGEKVVHMN
     NEAIDQGVRA IVEISLPASW EKAQDESKTE KEVPAFIKDV LIPMNRQEGD QLPVSAFLGR
     EDGAYPMGTS AYEKRGIAIN IPSWLPDHCI QCNQCSYVCP HAAIRPVLVN EEEMKNAPAG
     FVSKPAVGAK GMYFRMAISA YDCTGCGNCA QVCPAKQKAL EMKPLETQLE QAGLWEYALA
     LASKNNPVSP LTVKGSQFEQ PLLEFSGACA GCGETPYAKL VTQLFGDRMV VANATGCSSV
     WGASAPSMPY TTNKRGHGPA WGNSLFEDNA EYGLGMFLGA KQLRAKLAQE VTAAAELSLG
     AEFKTACEDW LVNMDRGEGT RARADKLTAL LEKSKGQDTL LNEIYKKKDF MVKRSQWIFG
     GDGWAYDIGF GGLDHVLASG QDVNVLVFDT EVYSNTGGQS SKSTPTAAIA KLAAGGKRTK
     KKDLGMMAIS YGYVYVAQIA MGADKNQTLK AMAEAEAYPG PSLIIAYAPC INHGLKAGMG
     GSQSEAKRAV ESGYWSLYRY NPQLKDTGKP VFTLDSKEPT MNFLEFLLGE VRYASMRKQF
     PELAEGLFKQ AEKEAADRLE GYRRLAGQ
//
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