ID W2CN31_9BACT Unreviewed; 1163 AA.
AC W2CN31;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:ETK08619.1};
GN ORFNames=T230_06720 {ECO:0000313|EMBL:ETK08619.1};
OS Tannerella sp. oral taxon BU063 isolate Cell 1/3.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=1411022 {ECO:0000313|EMBL:ETK08619.1, ECO:0000313|Proteomes:UP000034982};
RN [1] {ECO:0000313|EMBL:ETK08619.1, ECO:0000313|Proteomes:UP000034982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cell 1/3 {ECO:0000313|EMBL:ETK08619.1};
RA Beall C.J., Campbell A.G., Griffen A.L., Podar M., Leys E.J.;
RT "Single cell genomics of uncultured Tannerella BU063 (oral taxon 286).";
RL Submitted (NOV-2013) 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:ETK08619.1}.
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DR EMBL; AYYE01000905; ETK08619.1; -; Genomic_DNA.
DR AlphaFoldDB; W2CN31; -.
DR PATRIC; fig|1411022.3.peg.631; -.
DR Proteomes; UP000034982; 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 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:ETK08619.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 660..690
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 714..734
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 669
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 672
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 675
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 679
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 723
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 726
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 729
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 733
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 793
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 796
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 821
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 1057
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 12
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 45
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 95
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 982
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1163 AA; 128647 MW; AFEDB9B8EF1D9DCC CRC64;
MFSEVAAIYP ITPSSTMAEY VDEWAAAGRK NIFGETVLVQ EMQSEGGAAG AVHGSLQAGA
LTSTYTASQG LLLMIPNMYK IAGEFLPCVF HVSARTLASH ALSIFGDHQD VMAVRQTGFA
MLAEGSVQEV MDLAGVAHLA TLKSRIPFVS FFDGFRTSHE IQKIEKLDNE DLAPLIDQKA
LAEFRARALN PMNPVARGMA ENPDHFFQHR EAGNRFYDEV PAIVEEYMEE IYKLTGRKYG
LFNYYGAEDA DRVIIAMGSV TEAAREAIDY LVANGEKVGM VAVHLYRPFS AKHFLAAVPK
TVKRIAVLDR TKEPGANGEP LYLDVKDCFY GRENAPIIVG GRYGLSSKDT TPAQIISVFE
NLALNEPKNH FTVGIVDDVT FTSLPMKEEI ALGGEGMFEA KFYGLGADGT VGANKNSVKI
IGDNTDKYCQ AYFSYDSKKS GGFTCSHLRF GDHPIRSTYL VNTPNFVACH VQAYLHMYDV
TRGLRKNGSF LLNTIWEGDD LVRNLPVKVK KYFAKNNITV YYMNATEIAQ QIGLGNRTNT
ILQSAFFRIT GVIPVDLAVE QMKKFIVKSY GRKGEDVVNK NYAAVDRGGE YKQLTVDPAW
ADLPDDPRAA NSDPAFINEV VRTINAQDGD QLPVSAFKGR EDGTWMQGTA YYEKRGVATF
VPEWNMDNCI QCNQCAYVCP HAAIRPFVLD EEEQKGANFP QLKAQGKTFA GMNFRIQVDV
LDCTGCSNCV DVCPGKKGEK ALGMKHLETQ MDQVPNWNYC VDHVKTKQHL VDTKANAKNS
QFATPLFEFS GACAGCGETP YVKLVTQLYG DREMVANATG CSSIYSGSVP STPYTKNDMG
RGPAWANSLF EDFCEFGLGM ELANEKMRER IVKLFKQAIE NEYTPAEAKE LMQAWIDNMF
DADKTKELAP QLEVMIDRGI KEADCSVCKE LKGLTQYLIK RSQWIIGGDG ASYDIGYGGL
DHVIASGKDV NILVLDTEVY SNTGGQSSKS TPVGAIAKFA AAGKRVRKKD LGLMATTYGY
VYVAQIAMGA DQAQTLRAIR EAEAYPGPSL IIAYSPCINH GLKAGMGKSQ TEEKQAVACG
YWQLWRYNPQ LEAEGKNPFI LDSKAPNFDE FQNFLKGEVR YASVMKQYPA EAAELFKAAE
ENARWRYRNY QRMASNEFWA LGQ
//
