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Database: UniProt
Entry: Q53046
LinkDB: Q53046
Original site: Q53046 
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   13-FEB-2019, entry version 124.
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
OS   4362 / NCIB 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
RT   rubrum: partial characterization of a mutant unaffected in nitrogen
RT   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 / NCIB 8255 / S1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G.,
RA   Reslewic S., Zhou S., Schwartz D.C.;
RT   "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC
RT   11170.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Oxidoreductase required for the transfer of electrons
CC       from pyruvate to flavodoxin, which reduces nitrogenase.
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=ABC23198.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   ProteinModelPortal; Q53046; -.
DR   SMR; Q53046; -.
DR   STRING; 269796.Rru_A2398; -.
DR   PRIDE; Q53046; -.
DR   EnsemblBacteria; ABC23198; ABC23198; Rru_A2398.
DR   GeneID; 3835832; -.
DR   KEGG; rru:Rru_A2398; -.
DR   PATRIC; fig|269796.9.peg.2500; -.
DR   eggNOG; ENOG4105D95; Bacteria.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   HOGENOM; HOG000266425; -.
DR   KO; K03737; -.
DR   OrthoDB; 10483at2; -.
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:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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   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; Nitrogen fixation; Oxidoreductase; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN         1   1191       Pyruvate-flavodoxin oxidoreductase.
FT                                /FTId=PRO_0000215556.
FT   DOMAIN      687    716       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      744    773       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       696    696       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       699    699       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       702    702       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       706    706       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       753    753       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       756    756       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       759    759       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       763    763       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       825    825       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       828    828       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL       853    853       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   METAL      1085   1085       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P94692}.
FT   CONFLICT    986    986       G -> A (in Ref. 1; CAA54651).
FT                                {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
//
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