NIFJ_NOSS1
ID NIFJ_NOSS1 Reviewed; 1199 AA.
AC Q06879;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Pyruvate-flavodoxin oxidoreductase;
DE EC=1.2.7.-;
GN Name=nifJ; OrderedLocusNames=alr2803;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8415612; DOI=10.1073/pnas.90.19.8812;
RA Bauer C.C., Scappino L., Haselkorn R.;
RT "Growth of the cyanobacterium Anabaena on molecular nitrogen: NifJ is
RT required when iron is limited.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8812-8816(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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 -!- INDUCTION: By iron deprivation.
CC -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L14925; AAC36818.1; -; Unassigned_DNA.
DR EMBL; BA000019; BAB74502.1; -; Genomic_DNA.
DR PIR; AD2156; AD2156.
DR PIR; I39613; I39613.
DR RefSeq; WP_010996954.1; NZ_RSCN01000003.1.
DR AlphaFoldDB; Q06879; -.
DR SMR; Q06879; -.
DR STRING; 103690.17131896; -.
DR PRIDE; Q06879; -.
DR EnsemblBacteria; BAB74502; BAB74502; BAB74502.
DR KEGG; ana:alr2803; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR OMA; YAACINH; -.
DR OrthoDB; 10483at2; -.
DR Proteomes; UP000002483; 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 2: Evidence at transcript level;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..1199
FT /note="Pyruvate-flavodoxin oxidoreductase"
FT /id="PRO_0000215551"
FT DOMAIN 699..728
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 755..784
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 708
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 711
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 714
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 718
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 764
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 767
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 770
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 774
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
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 841
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 866
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 1103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT CONFLICT 250
FT /note="F -> FF (in Ref. 1; AAC36818)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="G -> A (in Ref. 1; AAC36818)"
FT /evidence="ECO:0000305"
FT CONFLICT 515..519
FT /note="AAAHG -> RLLM (in Ref. 1; AAC36818)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="T -> I (in Ref. 1; AAC36818)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183..1184
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1199 AA; 132170 MW; D4A7116E1B881E17 CRC64;
MSQTFATIDG NEAVARVAYK LNEVIAIYPI TPSSAMGEWA DAWMAEGRPN LWGTVPSVVQ
MQSEGGAAGA VHGALQTGSL STTFTASQGL LLMIPNLYKI GGELTSMVVH VAARSLATHA
LSIFGDHSDV MAARGTGFAM LCSASVQESH DFALIAHAAT LDTRVSFLHF FDGFRTSHEV
QKVELLADDD VRSLINEDKI FAHRARALTP DSPLLRGTAQ NPDVFFQARE GANPYYNACP
AIVQGIMDKF GERTGRYYQI YEYHGASDAD RLIIIMGSGC ETVHETVDYL NARGEKVGVL
KVRLFRPWDV ERFVQALPHS VQAIAVLDRT KEPGSAGEPL YQDVVTAIHE GWVNKNNSPV
PSPQSPVPKI IGGRYGLSSK EFTPAMVKAV FDNLAQATPK NHFTIGINDD VTHTSLEYDP
SFSTEPDNVV RAMFYGLGSD GTVGANKNSI KIIGEGTDNY AQGYFVYDSK KSGSMTVSHL
RFGSQPIRST YLIDQANFIG CHHWGFLERI EVLNAAAHGA TILLNSPYNA ATVWENLPLK
VRLQILDKQL KLYVINANQV ARDSGMGGRI NTIMQVCFFA LAGVLPEVQA IAKIKQAIEK
TYGKKGVEVV RMNLQAVDQT LENLHEVKIP IEEKGKWIDE EALLSNQSPF STSAPKFVRD
VLGKIMVWQG DDLPVSTLPP DGTFPTGTAK WEKRNVAQEI PVWDTDICVQ CSKCVMVCPH
AAIRAKVYQP SELENAPPTF KSVDAKDRDF ANQKFTIQVA PEDCTGCAIC VNVCPAKNKS
EPSLKAINMA NQLPLREQER DNWDFFLNLP NPDRRNLKLN QIRQQQLQEP LFEFSGACAG
CGETPYVKLL TQLFGDRSVI ANATGCSSIY GGNLPTTPWT KNNDGRGPAW SNSLFEDNAE
FGFGYRLSLD KQAEFAAELL QQFSTEVGDN LVDSILKAPQ KTEADIWEQR QRIELLKQQL
DKIPTFDPNL KSKIQNLKSL ADYLVKKSVW IIGGDGWAYD IDFGGIDHVI ASGRNVNILV
MDTEVYSNTG GQSSKATPKA AVAKFAASGK PAQKKDMGLM AMNYGNVYVA SVALGAKDDQ
TLKAFLEAEA FDGPSIIIAY SHCIAHGINM TTGMNQQKAL VESGRWLLYR YNPLLQEQGK
NPLQLDMRSP TQSVEQSMYQ ENRFKMLTKS KPEVAKQLLE QAQAEVDARW QMYQYLASR
