ID A0A073CIX3_PLAAG Unreviewed; 1214 AA.
AC A0A073CIX3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN Name=nifJ {ECO:0000313|EMBL:KEI67827.1};
GN ORFNames=A19Y_2986 {ECO:0000313|EMBL:KEI67827.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI67827.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI67827.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI67827.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
CC -!- FUNCTION: Oxidoreductase required for the transfer of electrons from
CC pyruvate to flavodoxin. {ECO:0000256|PIRNR:PIRNR000159}.
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 Evidence={ECO:0000256|ARBA:ARBA00001122,
CC ECO:0000256|PIRNR:PIRNR000159};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR000159-50};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000256|PIRSR:PIRSR000159-50};
CC -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009032,
CC ECO:0000256|PIRNR:PIRNR000159}.
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DR EMBL; CM002803; KEI67827.1; -; Genomic_DNA.
DR RefSeq; WP_042155052.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CIX3; -.
DR STRING; 388467.A19Y_2986; -.
DR PATRIC; fig|388467.6.peg.2933; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_002569_0_0_3; -.
DR Proteomes; UP000027395; 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; cd03377; TPP_PFOR_PNO; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 4.10.780.10; Pyruvate-flavodoxin oxidoreductase, EKR domain; 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_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR02176; pyruv_ox_red; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF10371; EKR; 1.
DR Pfam; PF12838; Fer4_7; 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; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000159-50};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000159};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000159-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000159-
KW 50};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000159-50};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000159};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 691..720
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 747..776
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1187..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 65
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 115
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 700
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 703
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 706
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 710
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 756
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 759
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 762
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 766
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 830
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 833
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 835
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 858
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 858
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 980..983
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1009..1014
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1089
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 32
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 65
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 115
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 1014
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1214 AA; 133202 MW; B05EA2CD4707A4E2 CRC64;
MNTKNYATLD GNEAVARVAY RLSEVIAIYP ITPSSPMGEW ADAWASVGDK NLWGTVPAVV
EMQSEGGAAG AVHGALQAGS LTTTFTASQG LMLMLPNLYK IAGELTCAVI QVAARSLAAQ
GLSIFGDHSD VMAARATGFA LLCSASVQEA QDMALIAQAS TLESRIPFIH FFDGFRTSHE
VQKIELLEDS DIRELIDDKY VYEHRNRALT PDRPVLRGTA QNPDVYFQGR ETVNIFYDQT
PEIVQRAMDK LGQLTGRNYK LFEYHGAPDA ERVIILMGSG CETVHETVDY LNAQGEKLGV
LKVRLYRPWD GEQLIAALPE TVKAIAVLDR TKEPGSSGEP LYLDVVTAVQ EVMLGDNDTL
KAKIKNLKAL VGGRYGLSSK EFNPAMVKSV FENLAQTKPK NHFTIGINDD VSHTSLEYDP
SFSTEPDNVV RAMFYGLGAD GTVGANKNSI KIIGEETDNY AQGYFVYDSK KSGAVTVSHL
RFGPQPIRSI YLISKANFIG CHQWTFIERL DVLQCAMEGS TFLLNSPYGP DQVWEYLPLE
IQEDIVRKNL KFYVIDANKV ARDMGMGNRI NTIMQVCFFA LAKVLPREEA IAQIKKAIEK
TYGKKGAEIV RLNLKAVDET LEHLYEVNVA QANSALRRAE PVAVGAPTFV KEVEGMMIAG
RGDDLPVSKL PCDGTYPTGT SKWEKRNVAQ DIPVWDADVC IQCGKCVMVC PHATIRGKAY
DEAALENAPA SFKFTNVKDK AFTGEKFTIQ VAPEDCTGCG ICVDVCPAKN KSMPSRKAIN
MEPQLPLREQ EATNWDFFLG IPNPDRLKLR PDLIRQQQWQ EPLFEFSGAC GGCGETPYIK
LVTQLFGDRM IVANATGCSS IYGGNLPTTP WTTNADGRGP AWSNSLFEDN AEFGLGFRMS
IDKHAGFALE LLHKLGGEVG DNLVTQITDN AQKSEADIWE QRQRVVQLKE KLQGLNSPDA
QQLLSLADYL VKKSVWIIGG DGWAYDIGYG GLDHVIASGR NVNILVLDTE VYSNTGGQSS
KATPRGAVAK FAAGGKPSAK KDLGLIAMTY GNVYVASVAM GAKDEHTLKA FLEAEAYDGP
SIIIAYSHCI AHGINMTTAM THQKDLVESG RWLLYRYNPD LKEAGKNPLI LDSKSPKKTV
EASMYAENRF KMLTKSKPAD AKRLLKEAQE DVSTRWKMYE YMAARPLETK GNNGHSEGKS
APISEGKPPE TTPV
//