NIFJ_SYNY3
ID NIFJ_SYNY3 Reviewed; 1199 AA.
AC P52965;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative pyruvate-flavodoxin oxidoreductase;
DE EC=1.2.7.-;
GN Name=nifJ; OrderedLocusNames=sll0741;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Oxidoreductase required for the transfer of electrons from
CC pyruvate to flavodoxin. {ECO:0000305}.
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; BA000022; BAA10774.1; -; Genomic_DNA.
DR PIR; S77082; S77082.
DR AlphaFoldDB; P52965; -.
DR SMR; P52965; -.
DR IntAct; P52965; 2.
DR STRING; 1148.1006618; -.
DR PaxDb; P52965; -.
DR EnsemblBacteria; BAA10774; BAA10774; BAA10774.
DR KEGG; syn:sll0741; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR InParanoid; P52965; -.
DR OMA; NTVMQVC; -.
DR PhylomeDB; P52965; -.
DR Proteomes; UP000001425; 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 GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
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..1199
FT /note="Putative pyruvate-flavodoxin oxidoreductase"
FT /id="PRO_0000215558"
FT DOMAIN 681..710
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 737..766
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
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 746
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 749
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 756
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 820
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 823
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 848
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 1079
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P94692"
SQ SEQUENCE 1199 AA; 131457 MW; 12F5C34C3B8D50B6 CRC64;
MSLPTYATLD GNEAVARVAY LLSEVIAIYP ITPSSPMGEW SDAWAAEHRP NLWGTVPLVV
EMQSEGGAAG TVHGALQSGA LTTTFTASQG LMLMLPNMHK IAGELTAMVL HVAARSLAAQ
GLSIFGDHSD VMAARNTGFA MLSSNSVQEA HDFALIATAT SFATRIPGLH FFDGFRTSHE
EQKIELLPQE VLRGLIKDED VLAHRGRALT PDRPKLRGTA QNPDVYFQAR ETVNPFYASY
PNVLEQVMEQ FGQLTGRHYR PYEYCGHPEA ERVIVLMGSG AETAQETVDF LTAQGEKVGL
LKVRLYRPFA GDRLVNALPK TVQKIAVLDR CKEPGSIGEP LYQDVLTAFF EAGMMPKIIG
GRYGLSSKEF TPAMVKGVLD HLNQTNPKNH FTVGINDDLS HTSIDYDPSF STEADSVVRA
IFYGLGSDGT VGANKNSIKI IGEDTDNYAQ GYFVYDSKKS GSVTVSHLRF GPNPILSTYL
ISQANFVACH QWEFLEQFEV LEPAVDGGVF LVNSPYGPEE IWREFPRKVQ QEIIDKNLKV
YTINANDVAR DAGMGRRTNT VMQTCFFALA GVLPREEAIA KIKQSVQKTY GKKGQEIVEM
NIKAVDSTLA HLYEVSVPET VSDDAPAMRP VVPDNAPVFV REVLGKIMAR QGDDLPVSAL
PCDGTYPTAT TQWEKRNVGH EIPVWDPDVC VQCGKCVIVC PHAVIRGKVY EEAELANAPV
SFKFTNAKDH DWQGSKFTIQ VAPEDCTGCG ICVDVCPAKN KSQPRLRAIN MAPQLPLREQ
ERENWDFFLD LPNPDRLSLN LNKISHQQMQ EPLFEFSGAC AGCGETPYLK LVSQLFGDRM
LVANATGCSS IYGGNLPTTP WAQNAEGRGP AWSNSLFEDN AEFGLGFRVA IDKQTEFAGE
LLKTFAGELG DSLVSEILNN AQTTEADIFE QRQLVEQVKQ RLQNLETPQA QMFLSVADYL
VKKSVWIIGG DGWAYDIGYG GLDHVLASGR NVNILVMDTE VYSNTGGQAS KATPRAAVAK
FAAGGKPSPK KDLGLMAMTY GNVYVASIAM GAKNEQSIKA FMEAEAYPGV SLIIAYSHCI
AHGINMTTAM NHQKELVDSG RWLLYRYNPL LADEGKNPLQ LDMGSPKVAI DKTVYSENRF
AMLTRSQPEE AKRLMKLAQG DVNTRWAMYE YLAKRSLGGE INGNNHGVSP SPEVIAKSV
