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Database: UniProt
Entry: A0PZX5_CLONN
LinkDB: A0PZX5_CLONN
Original site: A0PZX5_CLONN 
ID   A0PZX5_CLONN            Unreviewed;      1168 AA.
AC   A0PZX5;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   25-APR-2018, entry version 84.
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:ABK60855.1};
GN   OrderedLocusNames=NT01CX_1854 {ECO:0000313|EMBL:ABK60855.1};
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK60855.1, ECO:0000313|Proteomes:UP000008220};
RN   [1] {ECO:0000313|EMBL:ABK60855.1, ECO:0000313|Proteomes:UP000008220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT {ECO:0000313|EMBL:ABK60855.1,
RC   ECO:0000313|Proteomes:UP000008220};
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A.,
RA   Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W.,
RA   Vogelstein B., Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium
RT   novyi-NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK60855.1; -; Genomic_DNA.
DR   RefSeq; WP_011721931.1; NC_008593.1.
DR   ProteinModelPortal; A0PZX5; -.
DR   STRING; 386415.NT01CX_1854; -.
DR   EnsemblBacteria; ABK60855; ABK60855; NT01CX_1854.
DR   GeneID; 4541831; -.
DR   KEGG; cno:NT01CX_1854; -.
DR   PATRIC; fig|386415.7.peg.956; -.
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   OrthoDB; POG091H02IV; -.
DR   BioCyc; CNOV386415:G1G6M-974-MONOMER; -.
DR   Proteomes; UP000008220; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008220};
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:ABK60855.1}; Pyruvate {ECO:0000313|EMBL:ABK60855.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008220};
KW   Transport {ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN      679    708       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      735    766       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   COILED      889    913       {ECO:0000256|SAM:Coils}.
FT   METAL       688    688       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       691    691       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       694    694       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       698    698       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       810    810       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       813    813       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       838    838       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL      1069   1069       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   SITE         30     30       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE         63     63       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        113    113       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        994    994       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1168 AA;  127940 MW;  9BCC9DEF922CA41C CRC64;
     MAKMKTMDGN TAAAYTSYAF TDVTAIYPIT PSSPMAESVD EWSAQGKKNL FGQTVKVMEL
     QSEAGASAAV HGSLQSGALT TTYTASQGLL LMIPNMYKIA GELLPSVFHV SARALASHAL
     SIFGDHQDVM AARQTGFALL ASNSVQESMD LAAVAHLAAL KGRVPFVHFF DGFRTSHEIQ
     KVELLDYEDL RGLIDQDALK AFRNNALSPE HPVTRGTAQN PDIFFQAREA SNKYYNAIPG
     IVEEYMGEIN KITGRDYKLF NYYGAEDADR VIVAMGSGCE TIEEVVDYLS ARGEKVGLVK
     VHLYRPFSKE HLINAVPKTV KKIAVLDRTK EPGALGEPLY LDVKSAFYDV ENKPVIVGGR
     YGLGSKDTTP GQMAAVFENL KQDEPKNNFT LGINDDVTHT SLETVEGIDV VAEGTTACKF
     WGLGSDGTVG ANKSAIKIIG DHTDMYAQGY FAYDSKKSGG ITISHLRFGK SPIKSPYLIQ
     TPHFVACHNQ SYVNKYDVLE GLRDNGNFLL NCIWNQEEVE EHLPAHMKRY IANHNINFYT
     IDAVKIAQEI GLGGRINMIM QAAFFKLANI IPIEDAVKYL KDAVVTSYGK KGEKVVNMNH
     AAIDQGVGAI VKVEVPESWK TAEDKKVEEK DVPEFISKIL EPMNRQKGDE LPVSAFEGME
     DGTFPNGTAA YEKRGIAISV PEWSMENCIQ CNQCSYVCPH AVIRPTLLTE EEYNNKPEGF
     KAVEAKGIKG EKLYYAMNVS VLDCTGCGNC AEVCPAPTKA LVMKPAATQE AEQANYDYAQ
     TLSVKENPMD KYTVKGSQFE KPLLEFHGAC GGCGEAAYAK LITQLFGDRM MIANATGCTS
     IWGGSAPATP YTKNHEGKGP AWANSLFEDN AEYGLGMALG VSTIRTNMEN VAKEAMEEVS
     AELKSALQEW VDNKEDAEGS KKAAAKLLPL LEAEKSNAKV AEILENKDFL IKRSQWIFGG
     DGWAYDIGYG GVDHALASGE DINIFVFDTE VYSNTGGQSS KSTRTGAVAK FAAAGKRTKK
     KDLGLMAMTY GYVYVAQIAM GSDKNQTIKA IKEAEAYPGP SLIIAYAPCI NHGLKVGMAC
     SQLEEKKAVD CGYWGLYRYN PQLKEEGKNP FILDSKEPKG NFKDFLLGEV RYASLKKARP
     EQADELYAQT EKDAMERLET YKRLAEDK
//
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