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Database: UniProt
Entry: C7GZF3_9FIRM
LinkDB: C7GZF3_9FIRM
Original site: C7GZF3_9FIRM 
ID   C7GZF3_9FIRM            Unreviewed;      1189 AA.
AC   C7GZF3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
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:EEU03093.1};
GN   ORFNames=GCWU000322_00363 {ECO:0000313|EMBL:EEU03093.1};
OS   Eubacterium saphenum ATCC 49989.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=592031 {ECO:0000313|EMBL:EEU03093.1, ECO:0000313|Proteomes:UP000018436};
RN   [1] {ECO:0000313|EMBL:EEU03093.1, ECO:0000313|Proteomes:UP000018436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49989 {ECO:0000313|EMBL:EEU03093.1,
RC   ECO:0000313|Proteomes:UP000018436};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2009) 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:EEU03093.1}.
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DR   EMBL; ACON01000003; EEU03093.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7GZF3; -.
DR   STRING; 592031.GCWU000322_00363; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1013; Bacteria.
DR   eggNOG; COG1014; Bacteria.
DR   HOGENOM; CLU_002569_0_0_9; -.
DR   Proteomes; UP000018436; 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}; Pyruvate {ECO:0000313|EMBL:EEU03093.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018436};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN          692..721
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          748..779
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         41
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         74
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         124
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         701
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         704
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         707
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         711
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         757
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         760
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         763
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         767
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         823
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         826
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         828
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         851
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         851
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         979..982
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         1008..1013
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         1088
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   SITE            41
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            74
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            124
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            1013
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ   SEQUENCE   1189 AA;  130568 MW;  39A5030D697A64F6 CRC64;
     MGRSLWNKEV VMSNMKTMDG NTAAAYTSYA FTEVAAIYPI TPSSPMAELV DDWSARGRKN
     IFGQPVKVVE MQSEGGASGA LHGSLASGAL TSTYTASQGL LLMIPNMYKI SGELLPGVMH
     VTARALASHA LSIFGDQADV MSTRQTGFAM LASASVQEVM DLAAVAHLAA IKGRVPFLHF
     FDGFRTSHEI QKIETLDYDE LKKLVDMDAV KEFRHRALNP EHPVVRGSAQ NPDIYFQARE
     AANRYYEAVP EIVIEYMKEI EKLTGRKYNP FDYVGAEDAE YVVVAMGSVC EAIEETIERL
     VKAGKKVGLI KVRLYRPFVK ELFLGALPDT VKKIAVLDRT KEPGAFGEPL YEEIKAVLYG
     SENAPQVIGG RYGLGSKDVT PGMIEAVYKN LESTEPKDDF TIGINDDVTN KSLEYDASVT
     GEPEGTIRCM FWGLGSDGTV GANKTAIKII GDNTDMYAQG YFAYDSKKSG GVTISHLRFG
     KERIKSTYLI NNADFVACHN QAYLTQYDML KNLKKGGTFL LNTTWEGPEI EANIPGAVKR
     ELAQKKAKLY TINAVKIAEE IGLGHRINMV MQAAFFKLSK VLNLDDAVKY LKEGIDATYG
     RKGQNIVDMN CKAVDMGINA LSEHEVPAEW INAKDDDKAN ATSGKPEFIT KILEPMNKQE
     GDSLPVSLFK DRADGEFPTG TTQYEKRGVA VNVPTWRSET CIQCNQCAFV CPHACIRPVL
     VDADEKAKAP SQFKTEAAKG KGFEGLEFRM QVSPLDCLGC GSCANVCPTK EKSLVMTPLA
     DNMDEKENWE YAMEIPEKDN IMEKTSVKGS QFAKPYLEFS GACAGCGETP YIKVVTQLFG
     DRMVIANATG CSSIWGASAP SMPYCKDRNG KGPAWANSLF EDNAEYGLGI ATGIKQIRAR
     VKELLSELAS LNISKELKDA ISAWIENMEN SDVTRKVSDD LAKALKAEKV SGGREKELID
     VLIDLEDQFV KKSVWSVGGD GWAYDIGYGG LDHVLASGEN INVLVFDTEV YSNTGGQASK
     ATPTAAVAKF ASAGKRIKKK DLAKIAMAYG YVYVAQVGMG ADKNQFMKAI KEAEAYDGPS
     IIICYAPCIS HGIKTGMSTS QTNIKEAVDC GYWHLFRYNP LLEEQGKNPF VLDSKQPKES
     FREFLMGQVR YESLKKAFPD VAEGLFEQTE REAKKKYEDY AKMAGRSIE
//
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