ID Q831F2_ENTFA Unreviewed; 1177 AA.
AC Q831F2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase family protein {ECO:0000313|EMBL:AAO82270.1};
GN OrderedLocusNames=EF_2559 {ECO:0000313|EMBL:AAO82270.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO82270.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO82270.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO82270.1; -; Genomic_DNA.
DR RefSeq; NP_816200.1; NC_004668.1.
DR RefSeq; WP_010714077.1; NZ_KE136528.1.
DR AlphaFoldDB; Q831F2; -.
DR STRING; 226185.EF_2559; -.
DR EnsemblBacteria; AAO82270; AAO82270; EF_2559.
DR KEGG; efa:EF2559; -.
DR PATRIC; fig|226185.45.peg.993; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_002569_0_0_9; -.
DR Proteomes; UP000001415; Chromosome.
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 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:AAO82270.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001415};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 682..711
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 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 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 701
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 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 1073
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 28
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 61
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 111
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 998
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1177 AA; 130474 MW; 3CBFAEFD8C3F3D1C CRC64;
MKKTMDGNTA AAYISYAFTE VAAIYPITPS STMAELVDEW AESGLKNIYG QKVQVIEMQS
EAGAAGVVHG SLKTGALTTT YTASQGLLLM IPNMYKIAGE LLPSVFHVAA RAVTTSALSI
FGDHGDVMAT RQTGFCMLAE SSVQEVMDLS AVAHLASLEG SLPFVNFFDG FRTSHELQKI
EVIDYDDLKE MVNQEAVTRF RMGGMNPNHP TVSGTAQNPD IHFQQRETVN KNYEEMPKIV
QKYMKKINNL RGTTYDLTDY YGVEDATEVI ISMGSASPVI KQTVDYLNQQ GRKVGFINIH
LYRPFPTENL LEKLPATVEK VAVLDRTKES GAEGEPLLLD VQSALYQHEN RPIVIGGRYG
LGSKDVAPNQ IKAIYDHLLL PFKELKQRFT VGIVDDVTYQ SLPEEPTLDL TPDTTFQAKF
WGFGSDGTVG ANKQAIKIIG DHTDLYAQAY FSYDSKKSGG LTVSHLRFGK EPITSTYLIE
QADFIACHNA SYLHKYDLLK GLKDGGTFLL NTICDQEKIH RLLPAKLKKY IGEHQIKFYI
INAVELARKV GLGRRINTVM STAFFEVTDI LTKEQYLPLL KEEVKKTYGK KSMEIVEKNY
QAIDATFESL QEIVVPEDWA TIVLEPENQE SEAPAFVTNI LEPINRQEGD QLTVSDLIEN
GMKGGAIPMG TAAYEKRGIA LEVPEWQMDK CTMCNECAFV CPHAAIRPFL ADEEELKEAP
AGFAMREMRG TDGLMYRIQV SLEDCTGCGL CVQACPVKDK AILMKPYETQ KEQAMNWAFA
MTLKQKANPV KKLSVKGSQF NQPLMEFSGA CEGCGETPYI KLLTQLFGDR MMIANATGCS
SIWGGSSPVT PYTTNECGQG PAWSNSLFED NAEYGYGMYI ANRTKRQHLA SLVEESLAKN
VGSDSLQALL NDWLEHMAEG EGTQQRATKL AAALSEEADE DPLLTKIYEQ KDLLVKTSQW
IVGGDGWAYD IGFSGIDHVL ASGEDVNIFV MDNEVYANTG GQTSKATPAS AIAKFSAGGK
HTSKKDLGMM AITYGNVYVA QVALGANSMQ TIKAIDEAER YPGPSIIIGY TPCINHGVKG
GMVRTLDQAK EAVESGYWPL YRYNPELVKK GKDPMVIDYK KTDFDKMRDF LEKQTRYSAL
HTIKQNQEVV EHLLDKTKED AIERSESYNK LVTHMKK
//
