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Database: UniProt
Entry: A6L6T4_BACV8
LinkDB: A6L6T4_BACV8
Original site: A6L6T4_BACV8 
ID   A6L6T4_BACV8            Unreviewed;      1181 AA.
AC   A6L6T4;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   12-SEP-2018, entry version 74.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   OrderedLocusNames=BVU_3787 {ECO:0000313|EMBL:ABR41398.1};
OS   Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / NBRC
OS   14291 / NCTC 11154).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=435590 {ECO:0000313|EMBL:ABR41398.1, ECO:0000313|Proteomes:UP000002861};
RN   [1] {ECO:0000313|EMBL:ABR41398.1, ECO:0000313|Proteomes:UP000002861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / NBRC 14291 / NCTC 11154
RC   {ECO:0000313|Proteomes:UP000002861};
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M.,
RA   Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P.,
RA   Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A.,
RA   Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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   -!- SIMILARITY: Belongs to the nifJ family.
CC       {ECO:0000256|PIRNR:PIRNR000159}.
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DR   EMBL; CP000139; ABR41398.1; -; Genomic_DNA.
DR   RefSeq; WP_005842154.1; NC_009614.1.
DR   ProteinModelPortal; A6L6T4; -.
DR   STRING; 435590.BVU_3787; -.
DR   EnsemblBacteria; ABR41398; ABR41398; BVU_3787.
DR   GeneID; 5304746; -.
DR   KEGG; bvu:BVU_3787; -.
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; UP000002861; 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:UP000002861};
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   Pyruvate {ECO:0000313|EMBL:ABR41398.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002861};
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      1078   1078       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       1003   1003       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1181 AA;  129296 MW;  E7358858FD190AB5 CRC64;
     MTKQKKFITC DGNQAAAHIS YMFSEVAAIY PITPSSTMAE YVDEWAAAGR KNIFGETVLV
     QEMQSEGGAA GAVHGSLQAG ALTTTYTASQ GLLLMIPNMY KIAGEFLPCV FHVSARTLAS
     HALCIFGDHQ DVMSCRQTGF AMLCEGSVQE VMDMAAVAHL ATIKSRVPFV NFFDGFRTSH
     EIQKIEMLEN EDLAGLIDQQ ALAEFRQRAL NPNNPVARGM AENPDHFFQH RESCNNFYEA
     VPAIVEEYMN EISKITGRPH GLFDYYGAED AERVIIAMGS VTEAAREAID YLMSKGEKVG
     LVSVHLYRPF SAKHFLAAVP KTAKTIAVLD RTKEPGANGE PLYLDVKDCF YGTENAPVIV
     GGRYGLGSKD TTPAQIIAVF KNLALPMPKN HFTVGIVDDV TFTSLPQEEE IALGGEGMFE
     AKFYGLGADG TVGANKNSVK IIGDNTDKHC QAYFSYDSKK SGGFTCSHLR FGDTPIRSTY
     LVNTPNFVAC HVQAYLHMYD VTRGLRKNGS FLLNTIWEGE ELAKNLPNKV KKYFAQNNIT
     VYYINATQIA QEIGLGNRTN TILQSAFFRI TGVIPVDLAV EQMKKFIVKS YGKKGEDVVN
     KNYAAVDRGG EYKQLAVDPA WANLEVEAPA ANNDPAFINE VVRPINAQDG DLLPVSAFKG
     IEDGTWEQGT AQYEKRGVAA FVPEWNAENC IQCNKCAYVC PHASIRPFVL DAEEQKGADF
     ETLKAVGKQF DGMTFRIQVD VLDCLGCGNC ADVCPGNPKK GGKALTMKHL ESQLSQAANW
     EYCAKNVKSK QHLVDIKANV KNSQFATPLF EFSGACSGCG ETPYVKLISQ LFGDREMVAN
     ATGCSSIYSG SVPSTPYTKN EKGQGPAWAN SLFEDFCEFG LGMTLADKKL RARIEAAMKD
     AIASDTCPAE YKEAFQEWID GKDDADKSKA AAEKIIPMVE AAKDKCKNCA TIAEFKNYLV
     KKSQWIIGGD GASYDIGYGG LDHVIASGED VNILVLDTEV YSNTGGQSSK ATPLGAIAKF
     AASGKRVRKK DLGMIATTYG YVYVAQIAMG ADQAQTLKAI REAEAYPGPS LVIAYAPCIN
     HGLKAGMGKS QAEEAKAVEC GYWHLWRFNP ALEEEGKNPF MLDSKEPKWE GFQDFLKNEV
     RFASVMKQYP AEAADLFAAC EEMAKKRYAS YKRMEAMNWG E
//
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