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Database: UniProt
Entry: P52647
LinkDB: P52647
Original site: P52647 
ID   NIFJ_ECOLI              Reviewed;        1174 AA.
AC   P52647; P77238;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   10-APR-2019, entry version 164.
DE   RecName: Full=Probable pyruvate-flavodoxin oxidoreductase;
DE            EC=1.2.7.-;
GN   Name=ydbK; OrderedLocusNames=b1378, JW1372;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
RC   STRAIN=K12;
RX   PubMed=9025293; DOI=10.1099/00221287-143-1-187;
RA   Bunch P.K., Mat-Jan F., Lee N., Clark D.P.;
RT   "The ldhA gene encoding the fermentative lactate dehydrogenase of
RT   Escherichia coli.";
RL   Microbiology 143:187-195(1997).
RN   [5]
RP   IDENTIFICATION.
RA   Rudd K.E.;
RL   Unpublished observations (MAR-1996).
CC   -!- FUNCTION: Oxidoreductase required for the transfer of electrons
CC       from pyruvate to flavodoxin. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + 2 H(+) + oxidized [flavodoxin] + pyruvate = acetyl-
CC         CoA + CO2 + reduced [flavodoxin]; Xref=Rhea:RHEA:44140,
CC         Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P94692};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit.
CC       {ECO:0000250|UniProtKB:P94692};
CC   -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=U36928; Type=Frameshift; Positions=35; Evidence={ECO:0000305};
DR   EMBL; U00096; AAC74460.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14982.1; -; Genomic_DNA.
DR   EMBL; U36928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; E64888; E64888.
DR   RefSeq; NP_415896.1; NC_000913.3.
DR   RefSeq; WP_000628244.1; NZ_LN832404.1.
DR   ProteinModelPortal; P52647; -.
DR   SMR; P52647; -.
DR   BioGrid; 4261676; 23.
DR   DIP; DIP-11636N; -.
DR   IntAct; P52647; 10.
DR   STRING; 511145.b1378; -.
DR   DrugBank; DB00698; Nitrofurantoin.
DR   EPD; P52647; -.
DR   jPOST; P52647; -.
DR   PaxDb; P52647; -.
DR   PRIDE; P52647; -.
DR   EnsemblBacteria; AAC74460; AAC74460; b1378.
DR   EnsemblBacteria; BAA14982; BAA14982; BAA14982.
DR   GeneID; 946587; -.
DR   KEGG; ecj:JW1372; -.
DR   KEGG; eco:b1378; -.
DR   PATRIC; fig|511145.12.peg.1440; -.
DR   EchoBASE; EB2975; -.
DR   EcoGene; EG13183; ydbK.
DR   eggNOG; ENOG4105D95; Bacteria.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   HOGENOM; HOG000266425; -.
DR   InParanoid; P52647; -.
DR   KO; K03737; -.
DR   PhylomeDB; P52647; -.
DR   BioCyc; EcoCyc:G6701-MONOMER; -.
DR   BioCyc; ECOL316407:JW1372-MONOMER; -.
DR   BioCyc; MetaCyc:G6701-MONOMER; -.
DR   PRO; PR:P52647; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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:0043873; F:pyruvate-flavodoxin oxidoreductase activity; IDA:EcoCyc.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
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; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Reference proteome; Repeat; Transport.
FT   CHAIN         1   1174       Probable pyruvate-flavodoxin
FT                                oxidoreductase.
FT                                /FTId=PRO_0000215557.
FT   DOMAIN      680    709       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      736    765       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       689    689       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       692    692       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       695    695       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       699    699       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       745    745       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       748    748       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       751    751       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       755    755       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       819    819       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       822    822       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       847    847       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL      1071   1071       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   CONFLICT     40     40       A -> R (in Ref. 4). {ECO:0000305}.
FT   CONFLICT     51     51       T -> S (in Ref. 4). {ECO:0000305}.
SQ   SEQUENCE   1174 AA;  128824 MW;  2BBD1112285DC0F8 CRC64;
     MITIDGNGAV ASVAFRTSEV IAIYPITPSS TMAEQADAWA GNGLKNVWGD TPRVVEMQSE
     AGAIATVHGA LQTGALSTSF TSSQGLLLMI PTLYKLAGEL TPFVLHVAAR TVATHALSIF
     GDHSDVMAVR QTGCAMLCAA NVQEAQDFAL ISQIATLKSR VPFIHFFDGF RTSHEINKIV
     PLADDTILDL MPQVEIDAHR ARALNPEHPV IRGTSANPDT YFQSREATNP WYNAVYDHVE
     QAMNDFSAAT GRQYQPFEYY GHPQAERVII LMGSAIGTCE EVVDELLTRG EKVGVLKVRL
     YRPFSAKHLL QALPGSVRSV AVLDRTKEPG AQAEPLYLDV MTALAEAFNN GERETLPRVI
     GGRYGLSSKE FGPDCVLAVF AELNAAKPKA RFTVGIYDDV TNLSLPLPEN TLPNSAKLEA
     LFYGLGSDGS VSATKNNIKI IGNSTPWYAQ GYFVYDSKKA GGLTVSHLRV SEQPIRSAYL
     ISQADFVGCH QLQFIDKYQM AERLKPGGIF LLNTPYSADE VWSRLPQEVQ AVLNQKKARF
     YVINAAKIAR ECGLAARINT VMQMAFFHLT QILPGDSALA ELQGAIAKSY SSKGQDLVER
     NWQALALARE SVEEVPLQPV NPHSANRPPV VSDAAPDFVK TVTAAMLAGL GDALPVSALP
     PDGTWPMGTT RWEKRNIAEE IPIWKEELCT QCNHCVAACP HSAIRAKVVP PEAMENAPAS
     LHSLDVKSRD MRGQKYVLQV APEDCTGCNL CVEVCPAKDR QNPEIKAINM MSRLEHVEEE
     KINYDFFLNL PEIDRSKLER IDIRTSQLIT PLFEYSGACS GCGETPYIKL LTQLYGDRML
     IANATGCSSI YGGNLPSTPY TTDANGRGPA WANSLFEDNA EFGLGFRLTV DQHRVRVLRL
     LDQFADKIPA ELLTALKSDA TPEVRREQVA ALRQQLNDVA EAHELLRDAD ALVEKSIWLI
     GGDGWAYDIG FGGLDHVLSL TENVNILVLD TQCYSNTGGQ ASKATPLGAV TKFGEHGKRK
     ARKDLGVSMM MYGHVYVAQI SLGAQLNQTV KAIQEAEAYP GPSLIIAYSP CEEHGYDLAL
     SHDQMRQLTA TGFWPLYRFD PRRADEGKLP LALDSRPPSE APEETLLHEQ RFRRLNSQQP
     EVAEQLWKDA AADLQKRYDF LAQMAGKAEK SNTD
//
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