ID   NIFJ_KLEPN              Reviewed;        1171 AA.
AC   P03833; P09112;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase;
DE            EC=1.2.7.-;
GN   Name=nifJ;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA   Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT   "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT   nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL   J. Mol. Biol. 203:715-738(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3060860; DOI=10.1093/nar/16.23.11379;
RA   Cannon M., Cannon F., Buchanan-Wollaston V., Alley D., Alley A., Beynon J.;
RT   "The nucleotide sequence of the nifJ gene of Klebsiella pneumoniae.";
RL   Nucleic Acids Res. 16:11379-11379(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=8483412; DOI=10.1111/j.1365-2958.1993.tb01192.x;
RA   Charlton W., Cannon W., Buck M.;
RT   "The Klebsiella pneumoniae nifJ promoter: analysis of promoter elements
RT   regulating activation by the NifA promoter.";
RL   Mol. Microbiol. 7:1007-1021(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-127.
RX   PubMed=6306580; DOI=10.1093/nar/11.12.4241;
RA   Shen S., Xue Z., Kong Q., Wu Q.;
RT   "An open reading frame upstream from the nifH gene of Klebsiella
RT   pneumoniae.";
RL   Nucleic Acids Res. 11:4241-4250(1983).
CC   -!- FUNCTION: Oxidoreductase required for the transfer of electrons from
CC       pyruvate to flavodoxin, which reduces nitrogenase.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X01007; CAA25502.1; -; Genomic_DNA.
DR   EMBL; X13303; CAA31665.1; -; Genomic_DNA.
DR   EMBL; X13109; CAA31501.1; -; Genomic_DNA.
DR   PIR; S01997; QQKBFP.
DR   AlphaFoldDB; P03833; -.
DR   SMR; P03833; -.
DR   PRIDE; P03833; -.
DR   BioCyc; MetaCyc:NIFJKLEB-MON; -.
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; IEA:RHEA.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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; PF12838; Fer4_7; 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   Nitrogen fixation; Oxidoreductase; Repeat; Transport.
FT   CHAIN           1..1171
FT                   /note="Pyruvate-flavodoxin oxidoreductase"
FT                   /id="PRO_0000215555"
FT   DOMAIN          682..711
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          736..767
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         691
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         694
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         697
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         701
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         811
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         814
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         839
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         1072
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   CONFLICT        406
FT                   /note="A -> R (in Ref. 2; CAA31501)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1171 AA;  128041 MW;  95796232AD11012C CRC64;
     MSGKMKTMDG NAAAAWISYA FTEVAAIYPI TPSTPMAENV DEWAAQGKKN LFGQPVRLME
     MQSEAGAAGA VHGALQAGAL TTTYTASQGL LLMIPNMYKI AGELLPGVFH VSARALATNS
     LNIFGDHQDV MAVRQTGCAM LAENNVQQVM DLSAVAHLAA IKGRIPFVNF FDGFRTSHEI
     QKIEVLEYEQ LATLLDRPAL DSFRRNALHP DHPVIRGTAQ NPDIYFQERE AGNRFYQALP
     DIVESYMTQI SALTGREYHL FNYTGAADAE RVIIAMGSVC DTVQEVVDTL NAAGEKVGLL
     SVHLFRPFSL AHFFAQLPKT VQRIAVLDRT KEPGAQAEPL CLDVKNAFYH HDDAPLIVGG
     RYALGGKDVL PNDIAAVFDN LNKPLPMDGF TLGIVDDVTF TSLPPAQQTL AVSHDGITAC
     KFWGMGSDGT VGANKSAIKI IGDKTPLYAQ AYFSYDSKKS GGITVSHLRF GDRPINSPYL
     IHRADFISCS QQSYVERYDL LDGLKPGGTF LLNCSWSDAE LEQHLPVGFK RYLARENIHF
     YTLNAVDIAR ELGLGGRFNM LMQAAFFKLA AIIDPQTAAD YLKQAVEKSY GSKGAAVIEM
     NQRAIELGMA SLHQVTIPAH WATLDEPAAQ ASAMMPDFIR DILQPMNRQC GDQLPVSAFV
     GMEDGTFPSG TAAWEKRGIA LEVPVWQPEG CTQCNQCAFI CPHAAIRPAL LNGEEHDAAP
     VGLLSKPAQG AKEYHYHLAI SPLDCSGCGN CVDICPARGK ALKMQSLDSQ RQMAPVWDYA
     LALTPKSNPF RKTTVKGSQF ETPLLEFSGA CAGCGETPYA RLITQLFGDR MLIANATGCS
     SIWGASAPSI PYTTNHRGHG PAWANSLFED NAEFGLGMML GGQAVRQQIA DDMTAALALP
     VSDELSDAMR QWLAKQDEGE GTRERADRLS ERLAAEKEGV PLLEQLWQNR DYFVRRSQWI
     FGGDGWAYDI GFGGLDHVLA SGEDVNILVF DTEVYSNTGG QSSKSTPVAA IAKFAAQGKR
     TRKKDLGMMA MSYGNVYVAQ VAMGADKDQT LRAIAEAEAW PGPSLVIAYA ACINHGLKAG
     MRCSQREAKR AVEAGYWHLW RYHPQREAEG KTPFMLDSEE PEESFRDFLL GEVRYASLHK
     TTPHLADALF SRTEEDARAR FAQYRRLAGE E