ID E1WU33_BACF6 Unreviewed; 1184 AA.
AC E1WU33;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Putative pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:CBW23670.1};
DE EC=1.2.7.- {ECO:0000313|EMBL:CBW23670.1};
GN Name=nifJ {ECO:0000313|EMBL:CBW23670.1};
GN OrderedLocusNames=BF638R_3194 {ECO:0000313|EMBL:CBW23670.1};
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW23670.1, ECO:0000313|Proteomes:UP000008560};
RN [1] {ECO:0000313|EMBL:CBW23670.1, ECO:0000313|Proteomes:UP000008560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R {ECO:0000313|EMBL:CBW23670.1,
RC ECO:0000313|Proteomes:UP000008560};
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(2010).
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; FQ312004; CBW23670.1; -; Genomic_DNA.
DR RefSeq; WP_005789619.1; NC_016776.1.
DR AlphaFoldDB; E1WU33; -.
DR GeneID; 66332016; -.
DR KEGG; bfg:BF638R_3194; -.
DR PATRIC; fig|862962.3.peg.3292; -.
DR HOGENOM; CLU_002569_0_0_10; -.
DR Proteomes; UP000008560; 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:CBW23670.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 681..711
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 735..763
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 690
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
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 700
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 744
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 747
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 750
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="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 816
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 844
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 1079
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 33
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 66
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 116
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 1004
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1184 AA; 129688 MW; 46D908677773468B CRC64;
MTKQKKFITC DGNQAAAHIS YMFSEVAAIY PITPSSTMAE YVDEWAAAGR KNIFGETVLV
QEMQSEGGAA GAVHGSLQAG ALTTTYTASQ GLLLMIPNMY KIAGEFLPCV FHVSARTLAS
HALCIFGDHQ DVMSARQTGF AMLAEGSVQE VMDLAGVAHL ATIKARVPFM NFFDGFRTSH
EIQKIEMLEN EDLAPLVDQE ALAEFRARAL NPMNPVARGM AENPDHFFQH RESCNNYYEA
VPAIVEEYMN EISKITGRKY GLFDYYGAED AERVIIAMGS VTEAAREAID YLTSQGEKVG
LVAVHLYRPF SAKHFLAAVP KTAKTIAVLD RTKEPGANGE PLYLDVKDCF YGAENAPVIV
GGRYGLGSKD TTPAQIIAVF KNLAMPMPKN HFTIGIVDDV TFTSLPQEAE IALGGEGMFE
AKFYGLGADG TVGANKNSVK IIGDNTDKHC QAYFSYDSKK SGGFTCSHLR FGDDPIRSTY
LVNTPNFVAC HVQAYLHMYD VTRGLRKNGS FLLNTIWEGE ELAKNLPNKV KKYFAQNNIS
VYYINATQIA QEIGLGNRTN TILQSAFFRI TGVIPVDQAV EQMKKFIVKS YGKKGEDVVN
KNYAAVDRGG EYKTLTVDPA WANLPDDAKV ENNDPAFINE VVRPINAQDG DLLPVSAFKG
IEDGTWYQGT SKYEKRGVAA FVPEWNAENC IQCNKCAYVC PHASIRPFVL DAEEQKGANF
EMLKAVGKQF DGMTFRIQVD VLDCLGCGNC ADICPGNPKK GGKALTMKHL ESQLAQADNW
TYCADNVKSK QHLVDIKANV KNSQFATPLF EFSGACSGCG ETPYVKLISQ LYGDREMVAN
ATGCSSIYSG SVPSTPYTTN AKGHGPAWAN SLFEDFCEFG LGMELANEKM RARIVKLFNE
ILAADNAPAE AKEVLKAWIE NMYDADKTKE LAPQIEAIIE QGIAAGCPIS KELKGLTQYL
VKRSQWIIGG DGASYDIGYG GLDHVIASGK DVNILVLDTE VYSNTGGQSS KATPVGAIAK
FAASGKRVRK KDLGLMATTY GYVYVAQIAM GADQAQTLKA IREAEAYPGP SLIIAYAPCI
NHGLKAGMGK SQEEEEKAVK CGYWHLWRYN PALEAEGKNP FTLDSKEPNW DDFKGFLKGE
VRYASVMKQY PAEAEELFQA AEDNAKWRYN NYKRLANQAW GAAE
//
