NIFJ_ENTAG
ID NIFJ_ENTAG Reviewed; 1173 AA.
AC P19543;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pyruvate-flavodoxin oxidoreductase;
DE EC=1.2.7.-;
GN Name=nifJ;
OS Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OG Plasmid pEA3.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX NCBI_TaxID=549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=333;
RA Schwickerath O.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
RC STRAIN=333;
RX PubMed=2504647; DOI=10.1016/0378-1119(89)90318-1;
RA Kreutzer R., Singh M., Klingmueller W.;
RT "Identification and characterization of the nifH and nifJ promoter regions
RT located on the nif-plasmid pEA3 of Enterobacter agglomerans 333.";
RL Gene 78:101-109(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1028-1173.
RC STRAIN=333;
RX PubMed=1708766; DOI=10.1128/jb.173.10.3252-3256.1991;
RA Kreutzer R., Dayananda S., Klingmueller W.;
RT "Cotranscription of the electron transport protein genes nifJ and nifF in
RT Enterobacter agglomerans 333.";
RL J. Bacteriol. 173:3252-3256(1991).
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}.
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DR EMBL; X78558; CAA55302.1; -; Genomic_DNA.
DR EMBL; X99694; CAA68011.1; -; Genomic_DNA.
DR EMBL; M26931; AAA24806.2; -; Genomic_DNA.
DR EMBL; M38221; AAA23386.1; -; Genomic_DNA.
DR PIR; B39414; B39414.
DR AlphaFoldDB; P19543; -.
DR SMR; P19543; -.
DR PRIDE; P19543; -.
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; Plasmid; Repeat; Transport.
FT CHAIN 1..1173
FT /note="Pyruvate-flavodoxin oxidoreductase"
FT /id="PRO_0000215554"
FT DOMAIN 681..710
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 735..766
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 922..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 690
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 693
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
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 700
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 744
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 747
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 750
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 754
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 810
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 813
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 838
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 1075
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
SQ SEQUENCE 1173 AA; 128246 MW; 0B35809565C5DE4B CRC64;
MPGKMKTMDG NTAAAYVSYA FTDVTAIYPI TPSTPMAESV DEWAAQGKKN LFGQTVKIME
MQSESGAAGA IHGALQAGAL ATTYTASQGL LLMTPNMYKI AGELLPAVFH VSARALATNS
LNIFGDHQDS YAVRHTGCAM LAESSVQQVM DLAAVAHLTA IKGRIPFINF FDGFRTSHEI
QKIEVLDYED LAHLLDRDAV ARFRQNALHP DHPVVRGTAQ NPDIYFQERE ASNKFYMALP
EMVESYMAKI SALTGREYHL FNYYGAPDAG RMIIAMGSVC ETIQETVDYL NARGEKVGVL
TVHLYRPFSL KHFFKYIPKS VSNIAVLDRT KEPGSLAEPL YLDVKSAFYN SDWRPVIVGG
RYALGGKDIL PSHIISIFDN LAAERPRDGF TVGINDDVTF TSLPLSDRDI DTSSSGTTAC
KFWGLGSDGT VGANKSAIKI IGDKTDMYAQ AYFAYDSKKS GGVTMSHLRF GHNPIRSPYL
IDKADFISCS QQSYVNKYHL LAGLKPGGTF LLNCSWDVAE LDEKLPVAMK RYIAANDIQF
YIVNAVGIAQ KLGLGGRFNM IMQSAFFKLA DIIPLTRAVE YLKQSIEHAY GNKGQKIVDM
NNLAVDSGIE SVVKISVPQA WKHLEDKVVS PKKLPAFIKD ILIPMNRQEG DSLPVSIFDG
IEDGTFPSGT SAYEKRGVAI NVPVWQTDKC TQCNQCAFIC PHAAIRPVLI SEEERQNAPA
GFSAKRASGT EDAWYRLAVS PLDCSGCGNC ADVCPVKGKA LSMQPLESQE HEIELWEYAL
SLTPKANPQN KFTVKGSQFE QPLLEFSGAC GGCGETPYAK LVTQLFGDRM MIANATGCSS
IWGASAPSIP YTTNHKGQGP TWANSLFEDN AEFGLGMLLG VDAIRDTLAT QVKAALDNAP
DVPLDAELSA CLSDWLANKD QGEGTRERAE KVGDTSGFAN AREKSRTPTV SMPHRDYLAN
GSHWIFGGDG WAYDIGFGGL DHVLASGKDV NVLVFDTEVY SNTGGQSSKS TPAAAIAQFA
CKKTRKKDLG MMAMSYGYVY VAQIAMGADK NQTLRAIAEA EAYPGPSLII AYAACINHGL
RIGMGCSQRE ARRAVEAGYW ANYRYHPELK EAGKNPFILD SEEPEEDFQA FLAGEVRYSS
LKKLYPEFAE FLFKKTEDDA RERLEGYKKL ASS
