NIFJ_ECOLI
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 03-AUG-2022, entry version 177.
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., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT 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RL Unpublished observations (MAR-1996).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 from
CC pyruvate to flavodoxin. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + 2 H(+) + oxidized [flavodoxin] + pyruvate = acetyl-CoA +
CC CO2 + reduced [flavodoxin]; Xref=Rhea:RHEA:44140, Rhea:RHEA-
CC 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; Evidence={ECO:0000305};
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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 AlphaFoldDB; 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 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 eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_002569_0_0_6; -.
DR InParanoid; P52647; -.
DR OMA; NTVMQVC; -.
DR PhylomeDB; P52647; -.
DR BioCyc; EcoCyc:G6701-MON; -.
DR BioCyc; MetaCyc:G6701-MON; -.
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 CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
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; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..1174
FT /note="Probable pyruvate-flavodoxin oxidoreductase"
FT /id="PRO_0000215557"
FT DOMAIN 680..709
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 736..765
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 689
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 692
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 695
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 699
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 745
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 748
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 751
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 755
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 819
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 822
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 847
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 1071
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT CONFLICT 40
FT /note="A -> R (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="T -> S (in Ref. 4)"
FT /evidence="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
