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Database: UniProt
Entry: Q5LAL0_BACFN
LinkDB: Q5LAL0_BACFN
Original site: Q5LAL0_BACFN 
ID   Q5LAL0_BACFN            Unreviewed;      1184 AA.
AC   Q5LAL0;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   25-APR-2018, entry version 95.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   Name=nifJ {ECO:0000313|EMBL:CAH08863.1};
GN   ORFNames=BF9343_3082 {ECO:0000313|EMBL:CAH08863.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 /
OS   NCTC 9343).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH08863.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH08863.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343
RC   {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G.,
RA   Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A.,
RA   Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N.,
RA   Line A., Lord A., Norbertczak H., Ormond D., Price C.,
RA   Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable
RT   gene expression.";
RL   Science 307:1463-1465(2005).
CC   -!- FUNCTION: Oxidoreductase required for the transfer of electrons
CC       from pyruvate to flavodoxin. {ECO:0000256|PIRNR:PIRNR000159}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + CoA + oxidized flavodoxin = acetyl-
CC       CoA + CO(2) + reduced flavodoxin. {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 nifJ family.
CC       {ECO:0000256|PIRNR:PIRNR000159}.
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DR   EMBL; CR626927; CAH08863.1; -; Genomic_DNA.
DR   RefSeq; WP_005789619.1; NC_003228.3.
DR   ProteinModelPortal; Q5LAL0; -.
DR   STRING; 272559.BF3168; -.
DR   EnsemblBacteria; CAH08863; CAH08863; BF9343_3082.
DR   KEGG; bfs:BF9343_3082; -.
DR   eggNOG; ENOG4105D95; Bacteria.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   HOGENOM; HOG000266425; -.
DR   KO; K03737; -.
DR   OMA; NTVMQVC; -.
DR   Proteomes; UP000006731; 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   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.920.10; -; 1.
DR   Gene3D; 4.10.780.10; -; 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-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|PIRSR:PIRSR000159-50};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006731};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000159};
KW   Iron {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000159,
KW   ECO:0000313|EMBL:CAH08863.1}; Pyruvate {ECO:0000313|EMBL:CAH08863.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW   Transport {ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN      681    711       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      735    763       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       690    690       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       693    693       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       696    696       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       700    700       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       744    744       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       747    747       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       750    750       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       754    754       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       816    816       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       819    819       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       844    844       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL      1079   1079       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   SITE         33     33       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE         66     66       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        116    116       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE       1004   1004       Important for catalytic activity.
FT                                {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
//
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