ID   P94692_DESAF            Unreviewed;      1232 AA.
AC   P94692;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   SubName: Full=Pyruvate-ferredoxin oxidoreductase;
GN   Name=por;
OS   Desulfovibrio africanus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=873;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCIB 8401;
RX   MEDLINE=97440114; PubMed=9294422;
RA   Pieulle L., Magro V., Hatchikian E.C.;
RT   "Isolation and analysis of the gene encoding the pyruvate-ferredoxin
RT   oxidoreductase of Desulfovibrio africanus, production of the
RT   recombinant enzyme in Escherichia coli, and effect of carboxy-terminal
RT   deletions on its stability.";
RL   J. Bacteriol. 179:5684-5692(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCIB 8401;
RA   Claude H.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-1232.
RX   MEDLINE=99140300; PubMed=10048931; DOI=10.1038/5870;
RA   Chabriere E., Charon M.H., Volbeda A., Pieulle L., Hatchikian E.C.,
RA   Fontecilla-Camps J.C.;
RT   "Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin
RT   oxidoreductase, free and in complex with pyruvate.";
RL   Nat. Struct. Biol. 6:182-190(1999).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-1232.
RX   MEDLINE=21625364; PubMed=11752578; DOI=10.1126/science.1066198;
RA   Chabriere E., Vernede X., Guigliarelli B., Charon M.H.,
RA   Hatchikian E.C., Fontecilla-Camps J.C.;
RT   "Crystal structure of the free radical intermediate of
RT   pyruvate:ferredoxin oxidoreductase.";
RL   Science 294:2559-2563(2001).
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DR   EMBL; Y09702; CAA70873.1; -; Genomic_DNA.
DR   PDB; 1B0P; X-ray; 2.31 A; A/B=2-1232.
DR   PDB; 1KEK; X-ray; 1.90 A; A/B=2-1232.
DR   PDB; 2C3M; X-ray; 1.84 A; A/B=2-1232.
DR   PDB; 2C3O; X-ray; 2.70 A; A/B=2-1232.
DR   PDB; 2C3P; X-ray; 2.33 A; A/B=2-1232.
DR   PDB; 2C3U; X-ray; 2.32 A; A/B=2-1232.
DR   PDB; 2C3Y; X-ray; 1.93 A; A/B=2-1232.
DR   PDB; 2C42; X-ray; 1.78 A; A/B=2-1232.
DR   PDB; 2PDA; X-ray; 3.00 A; A/B=2-1232.
DR   PDB; 2UZA; X-ray; 2.42 A; A/B=2-1232.
DR   PDBsum; 1B0P; -.
DR   PDBsum; 1KEK; -.
DR   PDBsum; 2C3M; -.
DR   PDBsum; 2C3O; -.
DR   PDBsum; 2C3P; -.
DR   PDBsum; 2C3U; -.
DR   PDBsum; 2C3Y; -.
DR   PDBsum; 2C42; -.
DR   PDBsum; 2PDA; -.
DR   DIP; DIP:29036N; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the alde...; IEA:InterPro.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR   InterPro; IPR011766; TPP_enzyme_bd_C.
DR   InterPro; IPR015941; Transketolase_C-like.
DR   Gene3D; G3DSA:3.40.920.10; Pyrv_Fd/Flavodoxin_OxRdtase; 1.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF10371; EKR; 1.
DR   Pfam; PF00037; Fer4; 2.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PIRSF; PIRSF000159; NifJ; 1.
DR   TIGRFAMs; TIGR02176; pyruv_ox_red; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Pyruvate.
SQ   SEQUENCE   1232 AA;  133680 MW;  55D84F536CCFFDBF CRC64;
     MGKKMMTTDG NTATAHVAYA MSEVAAIYPI TPSSTMGEEA DDWAAQGRKN IFGQTLTIRE
     MQSEAGAAGA VHGALAAGAL TTTFTASQGL LLMIPNMYKI SGELLPGVFH VTARAIAAHA
     LSIFGDHQDI YAARQTGFAM LASSSVQEAH DMALVAHLAA IESNVPFMHF FDGFRTSHEI
     QKIEVLDYAD MASLVNQKAL AEFRAKSMNP EHPHVRGTAQ NPDIYFQGRE AANPYYLKVP
     GIVAEYMQKV ASLTGRSYKL FDYVGAPDAE RVIVSMGSSC ETIEEVINHL AAKGEKIGLI
     KVRLYRPFVS EAFFAALPAS AKVITVLDRT KEPGAPGDPL YLDVCSAFVE RGEAMPKILA
     GRYGLGSKEF SPAMVKSVYD NMSGAKKNHF TVGIEDDVTG TSLPVDNAFA DTTPKGTIQC
     QFWGLGADGT VGANKQAIKI IGDNTDLFAQ GYFSYDSKKS GGITISHLRF GEKPIQSTYL
     VNRADYVACH NPAYVGIYDI LEGIKDGGTF VLNSPWSSLE DMDKHLPSGI KRTIANKKLK
     FYNIDAVKIA TDVGLGGRIN MIMQTAFFKL AGVLPFEKAV DLLKKSIHKA YGKKGEKIVK
     MNTDAVDQAV TSLQEFKYPD SWKDAPAETK AEPMTNEFFK NVVKPILTQQ GDKLPVSAFE
     ADGRFPLGTS QFEKRGVAIN VPQWVPENCI QCNQCAFVCP HSAILPVLAK EEELVGAPAN
     FTALEAKGKE LKGYKFRIQI NTLDCMGCGN CADICPPKEK ALVMQPLDTQ RDAQVPNLEY
     AARIPVKSEV LPRDSLKGSQ FQEPLMEFSG ACSGCGETPY VRVITQLFGE RMFIANATGC
     SSIWGASAPS MPYKTNRLGQ GPAWGNSLFE DAAEYGFGMN MSMFARRTHL ADLAAKALES
     DASGDVKEAL QGWLAGKNDP IKSKEYGDKL KKLLAGQKDG LLGQIAAMSD LYTKKSVWIF
     GGDGWAYDIG YGGLDHVLAS GEDVNVFVMD TEVYSNTGGQ SSKATPTGAV AKFAAAGKRT
     GKKDLARMVM TYGYVYVATV SMGYSKQQFL KVLKEAESFP GPSLVIAYAT CINQGLRKGM
     GKSQDVMNTA VKSGYWPLFR YDPRLAAQGK NPFQLDSKAP DGSVEEFLMA QNRFAVLDRS
     FPEDAKRLRA QVAHELDVRF KELEHMAATN IFESFAPAGG KADGSVDFGE GAEFCTRDDT
     PMMARPDSGE ACDQNRAGTS EQQGDLSKRT KK
//