ID A0A242HME5_9ENTE Unreviewed; 1177 AA. AC A0A242HME5; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 29-SEP-2021, entry version 15. DE SubName: Full=Pyruvate:ferredoxin (Flavodoxin) oxidoreductase {ECO:0000313|EMBL:OTO77039.1}; GN ORFNames=A5865_000913 {ECO:0000313|EMBL:OTO77039.1}; OS Enterococcus sp. 12E11_DIV0728. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1834168 {ECO:0000313|EMBL:OTO77039.1, ECO:0000313|Proteomes:UP000194680}; RN [1] {ECO:0000313|EMBL:OTO77039.1, ECO:0000313|Proteomes:UP000194680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12E11_DIV0728 {ECO:0000313|EMBL:OTO77039.1, RC ECO:0000313|Proteomes:UP000194680}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genomic Center for Infectious Diseases; RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P., RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus sp. 12E11_DIV0728."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. 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:OTO77039.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NGLY01000001; OTO77039.1; -; Genomic_DNA. DR EnsemblBacteria; OTO77039; OTO77039; A5865_000913. DR Proteomes; UP000194680; 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; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.920.10; -; 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-bd_C. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF10371; EKR; 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; SSF52518; SSF52518; 2. DR SUPFAM; SSF52922; SSF52922; 1. DR SUPFAM; SSF53323; SSF53323; 1. DR TIGRFAMs; TIGR02176; pyruv_ox_red; 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:OTO77039.1}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}. FT DOMAIN 687..716 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 741..772 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT METAL 696 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 699 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 702 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 706 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 750 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 753 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 756 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 760 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 816 FT /note="Iron-sulfur 3 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 819 FT /note="Iron-sulfur 3 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 844 FT /note="Iron-sulfur 3 (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50" FT METAL 1076 FT /note="Iron-sulfur 3 (4Fe-4S)" 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 1001 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2" SQ SEQUENCE 1177 AA; 130154 MW; 0B448B39A8C50364 CRC64; MMKTMKTMDG NTAAAHISYA FTEVAGIYPI TPSSTMAEVV DEWAEQGRKN IFNETVKVVE MQSEAGAAGT VHGSLKTGVL TTTYTASQGL LLMIPNMFKI AGELLPTVFH VAARAVSTNA LSIFGDHSDV MAARQTGFCM LAEGGVQEVM DLSAVAHLAS IEGKLPFMNF FDGFRTSHEL QKIEVLDYDD LKAMVNWEAL EEFRKLGMNP NRPNVSGTAQ NPDIHFQQRE TVNRYYDEMP AIVQKYMQKI NDLRGTNYDL TNYYGDPEAT EVIIAMGSAS PTIQQTVDYL NANGRKVGFI DIHLYRPFPA ENLLEKLPAT VEKVAVLDRT KEPGSDGEPL LLDVQSVLYR HTNRPIVIGG RYGIASKDVT PDQIVAVFDH LLVPINEMKQ RFTIGINDDV TNLSLPMGEV LDLTPTSTFQ AKFWGLGSDG TVGANKQAIK IIGNNTDYYA QAYFSYDSKK SGGLTNSHLR FGKEPILSIY NVEAADFVGC HNSAYIHQYD LVKGLKDGGT FLLNTVWTEE KVKQLLPSRI KRYLAEHNIN FYIINAMEIA QKTGLGGRIN QVMSTAFFEL TDILDHETYL PLLKAEVDAA YGKKSRTIVE RNWQAIDATV AELKKVEIPA EWAEIEVKPL FNKEDQEKPA YIRNILEPIN RQEGNALSVN DLIENGMLGG VMPSGTAAYE KRGIALEVPE WIPEACTMCN ECAFVCPHAA IRPFLADEEE MEAAPEGFIT RDMRGKDGFN YRIQVSLEDC TGCGLCVEAC PAKEKALVMK SYEDQKDQAV NWAFAMTLRQ KANPAKKFSV KGSQFEQPLL EFSGACAGCG ETPYVKLLTQ LFGDRMMVAN TTGCSSIWGG SAPATPYTVN EDGRGPAWSN SLFEDNAEYG LGMHMANQTK RNRLANKVMK ALENGVGSED TRAQLQGWMN HMLDGEGSQQ RAAKLRAVLG EETDEDLRSI LADHEMFAKP SQWIIGGDGW AYDIGFSGID HVLASGEDVN ILVMDNEVYA NTGGQMSKAT PSAAIAKFAA GGKKTKKKDL GMMAMTYRDV YVAQVAIEAN PTQALKAIQE AEAYPGPSLI IGYTPCINHG IRGGMSQSIE ESKEAVESGY WPLYRYDPVR AQKGKDPMRI DFKKADFSKM NAFLEGQTRF SALHNIKKDD ELVEEMLTQT VDDMEERAKS YTELTNK //