ID A0A174RV39_9FIRM Unreviewed; 1178 AA.
AC A0A174RV39;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=porA {ECO:0000313|EMBL:CUP89493.1};
GN Synonyms=nifJ {ECO:0000313|EMBL:RGN07899.1};
GN ORFNames=DW021_05720 {ECO:0000313|EMBL:RHL48829.1}, DW040_10480
GN {ECO:0000313|EMBL:RHK95157.1}, DW222_09810
GN {ECO:0000313|EMBL:RHH18617.1}, DW272_08930
GN {ECO:0000313|EMBL:RHG17166.1}, DW859_07570
GN {ECO:0000313|EMBL:RHC07511.1}, DWW07_06305
GN {ECO:0000313|EMBL:RGV65250.1}, DWY46_05565
GN {ECO:0000313|EMBL:RGR49885.1}, DWZ12_00385
GN {ECO:0000313|EMBL:RGQ07694.1}, DXB81_05235
GN {ECO:0000313|EMBL:RGN07899.1}, EAI82_12290
GN {ECO:0000313|EMBL:RYT65259.1}, ERS852394_00474
GN {ECO:0000313|EMBL:CUN56515.1}, ERS852533_02934
GN {ECO:0000313|EMBL:CUP89493.1}, ROSSTS7063_02863
GN {ECO:0000313|EMBL:VUX18659.1};
OS Blautia obeum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=40520 {ECO:0000313|EMBL:CUP89493.1, ECO:0000313|Proteomes:UP000095413};
RN [1] {ECO:0000313|Proteomes:UP000095409, ECO:0000313|Proteomes:UP000095413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUN56515.1,
RC ECO:0000313|Proteomes:UP000095409}, and 2789STDY5834921
RC {ECO:0000313|EMBL:CUP89493.1, ECO:0000313|Proteomes:UP000095413};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000261222, ECO:0000313|Proteomes:UP000265808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF14-23 {ECO:0000313|EMBL:RGV65250.1,
RC ECO:0000313|Proteomes:UP000265828}, AF25-21
RC {ECO:0000313|EMBL:RGR49885.1, ECO:0000313|Proteomes:UP000285839},
RC AF29-2BH {ECO:0000313|EMBL:RGQ07694.1,
RC ECO:0000313|Proteomes:UP000283585}, AF37-6AC
RC {ECO:0000313|EMBL:RHL48829.1, ECO:0000313|Proteomes:UP000285897},
RC AF39-4 {ECO:0000313|EMBL:RHK95157.1,
RC ECO:0000313|Proteomes:UP000284267}, AM18-2AC
RC {ECO:0000313|EMBL:RHH18617.1, ECO:0000313|Proteomes:UP000284024},
RC AM22-9LB {ECO:0000313|EMBL:RHG17166.1,
RC ECO:0000313|Proteomes:UP000284220}, AM37-4AC
RC {ECO:0000313|EMBL:RHC07511.1, ECO:0000313|Proteomes:UP000265808}, and
RC OM06-11AA {ECO:0000313|EMBL:RGN07899.1,
RC ECO:0000313|Proteomes:UP000261222};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RYT65259.1, ECO:0000313|Proteomes:UP000293506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Af_0058 {ECO:0000313|EMBL:RYT65259.1}, and af_0058
RC {ECO:0000313|Proteomes:UP000293506};
RX PubMed=30630933; DOI=.1126/science.aau5238;
RA Jiang X., Hall A.B., Arthur T.D., Plichta D.R., Covington C.T., Poyet M.,
RA Crothers J., Moses P.L., Tolonen A.C., Vlamakis H., Alm E.J., Xavier R.J.;
RT "Invertible promoters mediate bacterial phase variation, antibiotic
RT resistance, and host adaptation in the gut.";
RL Science 363:181-187(2019).
RN [4] {ECO:0000313|EMBL:VUX18659.1, ECO:0000313|Proteomes:UP000409147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ruminococcus_obeum_SSTS_Bg7063 {ECO:0000313|EMBL:VUX18659.1};
RA Hibberd C M., Gehrig L. J., Chang H.-W., Venkatesh S.;
RL Submitted (JUL-2019) 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; CYZD01000002; CUN56515.1; -; Genomic_DNA.
DR EMBL; CZBA01000021; CUP89493.1; -; Genomic_DNA.
DR EMBL; QSUB01000001; RGN07899.1; -; Genomic_DNA.
DR EMBL; QRSS01000001; RGQ07694.1; -; Genomic_DNA.
DR EMBL; QRUH01000003; RGR49885.1; -; Genomic_DNA.
DR EMBL; QRZI01000003; RGV65250.1; -; Genomic_DNA.
DR EMBL; QSHL01000004; RHC07511.1; -; Genomic_DNA.
DR EMBL; QRHZ01000004; RHG17166.1; -; Genomic_DNA.
DR EMBL; QRJH01000004; RHH18617.1; -; Genomic_DNA.
DR EMBL; QROE01000004; RHK95157.1; -; Genomic_DNA.
DR EMBL; QROS01000003; RHL48829.1; -; Genomic_DNA.
DR EMBL; RCXQ01000012; RYT65259.1; -; Genomic_DNA.
DR EMBL; CABHNB010000043; VUX18659.1; -; Genomic_DNA.
DR RefSeq; WP_005422381.1; NZ_WWVS01000012.1.
DR AlphaFoldDB; A0A174RV39; -.
DR GeneID; 79803710; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000095409; Unassembled WGS sequence.
DR Proteomes; UP000095413; Unassembled WGS sequence.
DR Proteomes; UP000261222; Unassembled WGS sequence.
DR Proteomes; UP000265808; Unassembled WGS sequence.
DR Proteomes; UP000265828; Unassembled WGS sequence.
DR Proteomes; UP000283585; Unassembled WGS sequence.
DR Proteomes; UP000284024; Unassembled WGS sequence.
DR Proteomes; UP000284220; Unassembled WGS sequence.
DR Proteomes; UP000284267; Unassembled WGS sequence.
DR Proteomes; UP000285839; Unassembled WGS sequence.
DR Proteomes; UP000285897; Unassembled WGS sequence.
DR Proteomes; UP000293506; Unassembled WGS sequence.
DR Proteomes; UP000409147; 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:CUP89493.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095409};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 685..714
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 739..770
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 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 697
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 700
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="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 1178 AA; 127690 MW; 2D0D17260498CF92 CRC64;
MARKMKTMDG NHAAAHASYA YSDVAAIYPI TPSSVMAEAT DEWATQGRKN IFGQEVQVTE
MQSEAGAAGA VHGSLAAGAL TTTYTASQGL LLMIPNLYKI AGEQLPGVIN VSARALASHA
LSIFGDHSDV MACRQTGCAM LCESSVQEVM DLTPVAHLAA IKGKVPFINF FDGFRTSHEI
QKIETWDYED LKDMADMDAI QAFRDHALNP NHPCQRGSAQ NPDIFFQARE ACNPFYDALP
AVVQEYMDKV NEKIGTDYKL FNYYGAEDAE HIIIAMGSVN DTIEETIDYL AAAGKKVGVV
KVRLYRPFCA QALIDAIPDS VKQISVLDRT KEPGALGEPL YLDVVAALKD SKFKDVKIFT
GRYGLGSKDT TPAQIVAVYE NTTKEKFTIG IVDDVTNLSL ETGAPIVTTP EGTTNCKFWG
LGADGTVGAN KNSIKIIGDN TDMYAQAYFD YDSKKSGGVT MSHLRFGKKP IKSTYLIHKA
NFVACHNPSY VNKYNMVQEL VDGGTFLLNC AWDMEGLEKH LPGQVKAFIA NHDIKFYTID
GVKIGIETGM GPTRINTILQ SAFFKLTGII PEEQAIELMK AAAKATYGRK GDDVVQKNWA
AIDAGAKQVV EVKVPESWKD AEDEGLFMAH ATHGAQEAQD FVNNIQCKIN AQEGNTLPVS
AFTEYVDGTT PSGTAAYEKR GIAVNVPVWQ PENCIQCNRC AYVCPHAAIR PVALTEEEAA
NAPEGMATLP MTGMKDYKFT MTVSAYDCTG CGSCANVCPG KKGAKALAME NMEANAGLQK
FFDYGRELPI KEDVIAKFKE TTVKGSQFKQ PLLEFSGACA GCGETPYAKL ITQLFGDRMY
IANATGCSSI WGNSSPSTPY TTNAKGQGPA WANSLFEDNA EFGYGMLLAQ RAIRDGLKAK
VEAVVADGKD EAVKEAGQEW LDTFAVGATN GAATDKLIAA LEACGCDAAK EILAQKNYLS
KKSQWIFGGD GWAYDIGFGG VDHVLASGRD INVMVFDTEV YSNTGGQSSK STPTGAIAQF
AAGGKETKKK DMASIAMSYG YVYVAQISMG ADFNQTVKAI AEAEAYPGPS LIIAYAPCIN
HGIKKGMAKA QTEEELAVKC GYWHNFRFNP AADKKFALDS KTPDMENYMD FLNGEVRYNS
LQRQNPEKAA RLFAKNESEA KARYAYLNKL VAMYGEEE
//
