ID A0A0C1U363_9CLOT Unreviewed; 1173 AA.
AC A0A0C1U363;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 {ECO:0000313|EMBL:KIE47284.1};
GN ORFNames=U732_1443 {ECO:0000313|EMBL:KIE47284.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE47284.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE47284.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE47284.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE47284.1}.
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DR EMBL; AYSO01000015; KIE47284.1; -; Genomic_DNA.
DR RefSeq; WP_039632439.1; NZ_AYSO01000015.1.
DR AlphaFoldDB; A0A0C1U363; -.
DR STRING; 29341.RSJ17_13010; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000031366; 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:UniProtKB-EC.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 679..708
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 736..767
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 688
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 691
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 694
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 698
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 745
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 748
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 751
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 755
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 811
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="[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="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 839
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 839
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 962..965
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 991..996
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1071
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 996
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1173 AA; 129346 MW; B442F2139680A4A5 CRC64;
MRKMKTMDGN TAAAHVAYAF TDVAAIYPIT PSSPMAEHCD EWAAQGRKNI FGQTVKMMEM
QSEAGAAGAV HGSLQAGALT TTFTASQGLL LMIPNMYKIA GELLPGVFHV SARALAAQAL
SIFGDHQDVM AARQTGYALL ATNSVQEVMD LSPVAHLAAL EGRVPFLHFF DGFRTSHEVQ
KIEAWDYETL AKFANKEAVE AFRSKALNPN NPVTRGTAQN PDIYFQAREA SNRFYHAIPE
TVEKYMEMIN KEIGTDYHLF NYYGAQDADR MIVAMGSVCD VIEETIDYLT ARGEKVGLLK
VHLYRPFSLE HFFKYIPKTV KKIAVLDRTK EPGSAGEPLY QDVRTAYYDI ENRPVIIGGR
YGLGSKDTTP SQIVTVFDHL NNESLKNGFT IGINDDVTHT SLETSREIRT TTDGTIECKF
WGLGSDGTVG ANKSAIKIIG DNTNMYAQAY FSYDSKKSGG ITVSHLRFGK KPIKSPYLIN
HANYVGCHNQ SYVNKYDVLS GIKDNGTFLL NCIWDKNELE AHLPASMKRY IAEHDIKFYT
INAVKIAEEI GLGGRINMIM QAAFFKLADI IPIEEAVEHL KKAVVASYGK KGEKVVKMNN
DAIDAGVNSI VKIEVPESWE NAQDEMKPIQ ERPDFIKNIV DVMNRQEGDK LPVSAFIDRE
DGTFEPGTAA FEKREIAINV PEWQPDKCIQ CNQCSYVCPH AVIRPFIGTE EDYKNAPKTL
DFVDAKGGKA FEGLKFNIGV SIQDCTGCGN CAQVCPAKEK ALIMKPIDTQ TKQVENWKFN
LSLPKMSNPM GVASVKGSQF ETPLLEFSGA CAGCGETPYA KLVTQLYGDR MMVANATGCS
SIWGGSAPST PYTVNHKGKG PAWANSLFED NAEFGLGMFL GVNQLRGKLE LAVKEAVNGN
ISEELKALFN EWLDKKDDAE ATKVLADKIL PFLEAGKDSA VLTEVYNKKD FFVKRSQWIF
GGDGWAYDIG YGGVDHVLAT GENVNVLVFD TEVYSNTGGQ SSKSTPTAAI AKFAAAGKRT
KKKDLGMMAM SYGYVYVAQI AMGADQNQTL KAIREAEAYD GPSLIIAYAP CINHGIKNGM
GATQLETKLA VQSGYWALYR YNPMLKEEGK NPFTLDSKEP TLSFRDYLMG EVRYASLAKT
FPEQAEKLFA KTEQDAKERL EGYKKLAAQD FSK
//
