NIFJ_TRIV2
ID NIFJ_TRIV2 Reviewed; 1190 AA.
AC Q3M8N0; Q53349;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Pyruvate-flavodoxin oxidoreductase;
DE EC=1.2.7.-;
GN Name=nifJ; OrderedLocusNames=Ava_3046;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-109.
RX PubMed=8352652;
RA Schmitz O., Kentemich T., Zimmer W., Hundeshagen B., Bothe H.;
RT "Identification of the nifJ gene coding for pyruvate:ferredoxin
RT oxidoreductase in dinitrogen-fixing cyanobacteria.";
RL Arch. Microbiol. 160:62-67(1993).
CC -!- FUNCTION: Oxidoreductase required for the transfer of electrons from
CC pyruvate to flavodoxin, which reduces nitrogenase. {ECO:0000250}.
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; CP000117; ABA22656.1; -; Genomic_DNA.
DR EMBL; S64520; AAB27766.2; -; Genomic_DNA.
DR AlphaFoldDB; Q3M8N0; -.
DR SMR; Q3M8N0; -.
DR STRING; 240292.Ava_3046; -.
DR PRIDE; Q3M8N0; -.
DR EnsemblBacteria; ABA22656; ABA22656; Ava_3046.
DR KEGG; ava:Ava_3046; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_002569_0_0_3; -.
DR OMA; NTVMQVC; -.
DR Proteomes; UP000002533; 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; Repeat; Transport.
FT CHAIN 1..1190
FT /note="Pyruvate-flavodoxin oxidoreductase"
FT /id="PRO_0000215553"
FT DOMAIN 687..716
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 743..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 752
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="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 758
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 762
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 826
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 829
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 854
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 1089
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT CONFLICT 101..109
FT /note="IAGELTPTV -> VARVQPPTT (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1190 AA; 131530 MW; 4C8966D06A2A8F24 CRC64;
MKNRTFATID GNEAVAQVVY QINEVIAIYP ITPSSPMAEW SDAWASEGKP NIWGTVPTVV
QMQSEGGVAG AVHGALQTGS LTTTFTASQG LLLMIPNMYK IAGELTPTVF HIAARSLAAQ
ALSIFGDHSD VMATRGTGFA MLCAASVQEA HDFALISTRI TLESRIPFLH FFDGFRTSHE
INKIELLTTE DFKGFIPNEL VIAHRSRALT PDKPVLRGTA QNPDVYFQAR ETVNPYYLAC
PEITQKVMDE FAQMTGRQYQ LFEYHGDPTA ERVIILMGSG CETVHETVDY LNALGEKVGV
IKVRLYQPFD SQRFIAALPT TTRGIAVLDR TKEPGASGEP LYLDVVTALY EKWGVGSLPT
VIGGRYGLSS KEFTPGMVKA VFDNLAATIP KNHFTIGIND DVSHTSLDYD PDFNIEPDNI
VRAIFYGLGA DGTVGANKNS IKIIGEETNN YAQGYFVYDS KKSGSVTVSH LRFGSQLIRS
TYLINKASFV ACHQWDFLEK FPILKDIVQG GTFLLNSPYD QDEVWERLPG KIQAQIQQKQ
LKVYVINAYK VAREAGMAGR INTVMQVCFF ALSNVLPREE AIAEIKKYIR KTYGKKGDQI
VQMNIKAVDT TLDNLHELVT REYSAPPQIP NHHYPLSPEG APPSSIPYIL GKMIAREGDE
LPVSALPNDG TYPTGTAKWE KRNIAQEIPV WDTDVCIQCG KCVMVCPHSV IRSKVYEPEQ
LENAPSTFKS ANAKDHDWHG LKFTIQVAAE DCTGCGICVD VCPAKNKAQP RKKAINMEPQ
LPLRQAEREN WDFFLSIPNP DRRELKLTHI NQQQMQEPLF EFSGACAGCG ETPYIKLGTQ
LFGDRMIVAN ATGCSSIYGG NLPTTPWTQN AAGRGPAWSN SLFEDNAEFG LGFRVSIDKQ
TEIASQLLQE LATVVGRELV DDILNNQQNN EAEIWEQRDR ISILKQKLQA LVNPELTSKA
QLLLSLADYL VKKSVWIIGG DGWAYDIGYG GLDHVLASGR NVNILVLDTE VYSNTGGQMS
KATPKGAVAK FASGGKPAAK KDLGLMAMTY GNVYVASVAM GAKDEHTLKA FLEAEAYSGT
SLIIAYSHCI AHGINLSTAM QNQKAAVDSG RWLLYRYHPD LVKQGKNPLQ LDSRTPKLPL
EESMYLENRF KMLTKINPEV AKELLKEAQT DVNLRWQMYQ YLAAREVTQG
