ID A0A1I0V203_9FIRM Unreviewed; 1181 AA.
AC A0A1I0V203;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=SAMN05216249_101117 {ECO:0000313|EMBL:SFA70379.1};
OS Acetitomaculum ruminis DSM 5522.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetitomaculum.
OX NCBI_TaxID=1120918 {ECO:0000313|EMBL:SFA70379.1, ECO:0000313|Proteomes:UP000198838};
RN [1] {ECO:0000313|EMBL:SFA70379.1, ECO:0000313|Proteomes:UP000198838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5522 {ECO:0000313|EMBL:SFA70379.1,
RC ECO:0000313|Proteomes:UP000198838};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOJY01000001; SFA70379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0V203; -.
DR STRING; 1120918.SAMN05216249_101117; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000198838; 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: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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
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:SFA70379.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198838};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 684..713
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 739..759
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 693
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 696
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="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 703
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 754
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 758
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 819
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 822
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 824
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 847
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 847
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 969..972
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 998..1003
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1078
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 1003
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1181 AA; 128554 MW; D5CDC8306E79B53B CRC64;
MARKMSTMDG NHAAAHASYA FTDVAAIYPI TPSSVMAEAT DEWATQGRKN IFGQTVQVTE
MQSEAGAAGT VHGSLTAGAL TTTYTASQGL LLMIPNLYKV AGEGLPGVFN VSARTLASHA
LCIFGDHSDV YACRQTGCAM LCESSVQEVM DLTPVAHLSA IKGKLPFINF FDGFRTSHEI
QKIETWDYED LKDMADMDAI DEFRRNALNP NHPCELGSAQ NPDIFFQTRE ACNGKYNNIT
EVVQMYMDKV NEKIGTDYKL FNYYGAADAE HVIVAMGSVC ETIEEVIDYM TAAGEKVGLV
KVRLYRPFSA EALVKAIPDS CKKITVLDRS KEPGAIGEPL YLDVVAALNK TKFDGVEIFR
GRYGLGSKDT TPAQIYSVYK NTEKKEFTIG IVDDVTNLSL DIIENINTAS ENTVSCKFWG
LGADGTVGAN KNSIKIIGNN TDMYAQAYFD YDSKKSGGVT ISHLRFGKEP IRSTYLISMA
NFVACHNPAY ITKYDMVQDI VDGGKFLLNC SWNSEELEKN LPGRVKKYIA EHNIELYTID
GIKIGKEIGL GGRINTVLQS AFFKLAGIIP EADAIKYMKE AAKATYGRKG DNIVQMNYDA
IDRGAQDVVK VDVPASWKDA VDDAAASEKP LEGKPEVLAF VNTIQKAVNS QSGNKLKVSE
VAAYEDGHTP SGTAAYEKRG VAVDIPVWDS ENCIQCNYCS YVCPHAVIRP VALTEDEVKA
APEGMKTIPL TGLKDKYQFT MTVSAYDCTG CGSCVNVCPG KKGNKALSMQ SFAENEGSQA
IYDYAVKLPK KADVFEKFKI DSVKGSQFRQ PLLEFSGACA GCGETPYVKL LTQLFGDRMY
IANATGCSSI WGNSSPSTPY TTTPEGKGPA WSNSLFEDAA EFGYGMFLAQ RALRDSLKIK
VEAIADKTSN GDVKAAAKEY IDTFGIGITN GDATDKLVAA LEAEGSQEAK EIIKDKDFLA
KKSQWIFGGD GWAYDIGFGG VDHVLASGQD INILVLDTEV YSNTGGQSSK STPTGAIAQF
AAAGKEVKKK NLAEIAMSYG YIYVAQVAMG SDYNQCVKAM AEAEAYPGPS LVICYAPCIN
HGIKIGMSKA QTEEKNAVEA GYWHLFRFNP ELVDKGEAGF ILDSKAPTGD YKAFLNGEVR
YNSLVRANPE RAEKLFDKSE KEARDKYSHL VKLVDFYGKT E
//
