ID   NIFJ_RHORT              Reviewed;        1191 AA.
AC   Q53046; Q2RRP7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase;
DE            EC=1.2.7.-;
GN   Name=nifJ; OrderedLocusNames=Rru_A2398;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8736535; DOI=10.1046/j.1365-2958.1996.5311054.x;
RA   Lindblad A., Jansson J., Brostedt E., Johansson M., Hellman U.,
RA   Nordlund S.;
RT   "Identification and sequence of a nifJ-like gene in Rhodospirillum rubrum:
RT   partial characterization of a mutant unaffected in nitrogen fixation.";
RL   Mol. Microbiol. 20:559-568(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABC23198.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X77515; CAA54651.1; -; Genomic_DNA.
DR   EMBL; CP000230; ABC23198.1; ALT_INIT; Genomic_DNA.
DR   PIR; S70963; S70963.
DR   RefSeq; YP_427485.1; NC_007643.1.
DR   AlphaFoldDB; Q53046; -.
DR   SMR; Q53046; -.
DR   STRING; 269796.Rru_A2398; -.
DR   PRIDE; Q53046; -.
DR   EnsemblBacteria; ABC23198; ABC23198; Rru_A2398.
DR   KEGG; rru:Rru_A2398; -.
DR   PATRIC; fig|269796.9.peg.2500; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1013; Bacteria.
DR   eggNOG; COG1014; Bacteria.
DR   HOGENOM; CLU_002569_0_0_5; -.
DR   OrthoDB; 10483at2; -.
DR   PhylomeDB; Q53046; -.
DR   Proteomes; UP000001929; 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; 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; 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; Reference proteome; Repeat; Transport.
FT   CHAIN           1..1191
FT                   /note="Pyruvate-flavodoxin oxidoreductase"
FT                   /id="PRO_0000215556"
FT   DOMAIN          687..716
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          744..773
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         696
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="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         702
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         706
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         753
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         756
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         759
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         763
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         825
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         828
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         853
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         1085
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   CONFLICT        986
FT                   /note="G -> A (in Ref. 1; CAA54651)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1191 AA;  127817 MW;  911A76574A0CA19D CRC64;
     MSVRKMVAID GNEACASVAY RVSEVAVIYP ITPSSTMGEL SDEWSAKGLT NIWGAVPQVV
     EMQSEGGAAG ACHGAIQTGS LGTTFTASQG LLLMIPNMYK IAGELTPFCM HVTARTLATH
     ALSIFGDQSD VMACRQTGFA ILASASVQEA HDLASVAHGA SLESRIPFLH FFDGFRTSHE
     VNKIELMTDD DLHAMIDDDL VAAHRARALT PDTPVTRGTA QNPDTFFQAQ EARNPFYDAC
     PAIVQSYMDR LAALTGRRYG LFDYVGHPQA ERVVVIMGSG AETVAETVDW LVARGEKIGV
     VKVRLFRPFS VDAFVAALPV SVRAIAVLDR CKESGAIGEP LYLDVVGALA RAKALGLRAG
     IVDPAVIGGR YGLSSKEFTP AMVKAIFDEL AKANPKQAFT VGIEDDVTHL SLSVDRSFRI
     ESADIKRSVF FGLGADGTVG ANKNSIKIIS DSPTIHGQGY FVYDSKKSGA ITISHLRFGP
     RPIRAPYLID EADFIACHHF SFLDKVDVLE TAAVGATLLL NSPHDKDTVW DALPRPVQQT
     IIDRDLKLFV IDANKVAQET GMGQRINTIM QTCFFALSGV MPRDEAIEEI KKAISKTYAR
     KSQKVIDANF AAVDQTLSRL QSVTIPGVLT GHALPPLVSA GAPDFVRNVT AVMLAGKGDS
     LPVSAMPVDG TWPTETARWE KRDIAQQVCS WDADLCIQCN KCVMVCPHAA LRVKAVPAEA
     AAALPASMNS TPYKGKDDLK GSAYVLALSP EDCTGCGICV EACPGKDKAT GARSLTMHAR
     EDVVSACKEN WEIFLDLPDV ARTSLRPTVK NSQFMTPLFE FSGACQGCGE TPYLKLLTQM
     WGDRLMIANA TGCSSIYGGN LPTSPYAKDA NGRGPAWSNS LFEDNAEFGL GFRLALDQHR
     SEAKRLLGAL APQLSGVLVD GLVANAANND EAAIAAQRER VVSLRAELGG LTGWQARALE
     GLADYLVEKV VWIVGGDGWA YDIGYGGLDH VISSGRNVNI LVMDTEVYSN TGGQQSKSTP
     IGASAKFSVA GKALPKKDLG QIAMANGHVY VASIAFGASD NQTLRALSEA VSYEGPSLII
     AYSHCIAHGY DLTCGLSQQK LAIETGYWPL YRFDPRKMGV GPALSLDGVQ PSRPIGDYMA
     NEGRFRIIRD ADPERYAMLL EAAEENVRSR WALLRQLAGV ADEQEGARAA Q