ID A0A5Q0BFW3_9GAMM Unreviewed; 1194 AA.
AC A0A5Q0BFW3;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
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:QFY42012.1};
GN ORFNames=F6R98_04710 {ECO:0000313|EMBL:QFY42012.1};
OS Candidatus Methylospira mobilis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Methylococcales; Methylococcaceae; Candidatus Methylospira.
OX NCBI_TaxID=1808979 {ECO:0000313|EMBL:QFY42012.1, ECO:0000313|Proteomes:UP000325755};
RN [1] {ECO:0000313|EMBL:QFY42012.1, ECO:0000313|Proteomes:UP000325755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shm1 {ECO:0000313|EMBL:QFY42012.1,
RC ECO:0000313|Proteomes:UP000325755};
RA Oshkin I.Y., Dedysh S.N., Miroshnikov K., Danilova O.V., Hakobyan A.,
RA Liesack W.;
RT "Ecophysiology of the spiral-shaped methanotroph Methylospira mobilis as
RT revealed by the complete genome sequence.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidoreductase required for the transfer of electrons from
CC pyruvate to flavodoxin. {ECO:0000256|PIRNR:PIRNR000159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxidized [flavodoxin] + pyruvate + CoA + 2 H(+) = reduced
CC [flavodoxin] + acetyl-CoA + CO2; 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:ARBA00048963,
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; CP044205; QFY42012.1; -; Genomic_DNA.
DR RefSeq; WP_153247997.1; NZ_CP044205.1.
DR AlphaFoldDB; A0A5Q0BFW3; -.
DR FunCoup; A0A5Q0BFW3; 82.
DR KEGG; mmob:F6R98_04710; -.
DR InParanoid; A0A5Q0BFW3; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000325755; 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:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:TreeGrafter.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProtKB-ARBA.
DR CDD; cd03377; TPP_PFOR_PNO; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR FunFam; 3.30.70.20:FF:000022; Pyruvate:ferredoxin (Flavodoxin) oxidoreductase; 1.
DR FunFam; 3.40.50.920:FF:000007; Pyruvate:ferredoxin (Flavodoxin) oxidoreductase; 1.
DR FunFam; 3.40.50.970:FF:000012; Pyruvate:ferredoxin (Flavodoxin) oxidoreductase; 1.
DR FunFam; 3.40.50.970:FF:000041; Pyruvate:ferredoxin (Flavodoxin) oxidoreductase; 1.
DR FunFam; 3.40.920.10:FF:000001; Pyruvate:ferredoxin (Flavodoxin) oxidoreductase; 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; IPR050722; Pyruvate:ferred/Flavod_OxRd.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000159}; Pyruvate {ECO:0000313|EMBL:QFY42012.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000325755};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 688..717
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 744..773
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
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 697
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
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 707
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 753
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 763
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 827
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 832
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 855
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 855
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 977..980
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1006..1011
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1086
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 1011
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1194 AA; 130224 MW; A02EBDD3BD4ECE6F CRC64;
MSPVQVTTLE GNEAVAYIAY RTNEICSIYP ITPSSTMAEL ADQWASEGKT NIWGNIPLVV
EMQSEAGAAG AVHGALQTGA LTTTFTASQG LLLMIPNMYK IAGELTPAVF HVAARALAAQ
GLSIFGDHSD VAAVRNTGFA QLASSSVQEA HDMALLAQAA TLESRIPFVH FFDGFRTSHE
VNKIELIGDE QIRALIDADR VREHRARGLN PDNPFIRGTA QNPDIYFQAR ETVNPFYQAL
PQIVQDKMDA LAALTGRQYR LFDYFGHPQA ERVAVIIGSG AQTLYETVDY LQRQGEKVGV
INVRLCLPFS SEHFLTALPA TTQSIALLDR VKLPGSSGEP LYGDVLTCLS EANADGRLPT
RGLPRIVGGR YGLSSKEFTP AMAKAVLDEL KKDNPKNHFT IGINDDITLT SLDYDPAFDI
EPDHVVRALF IGLGADGTVG ANKNSIKIIG ESTPLHAQGY FVYDSKKSGS RTVSHVRFGP
KPILSPYLIQ SASFIGCHQF GFVDKMDVLA NARDGATFLL DSPYGPDEVW QHLPQRLQRQ
IIDRKIAFYV IDASSVARAT GMGNRTNTIM QTCFFAISGV LPRDEAIAKI KQSIKKTYGK
KGDEVVNKNF LAVDRTLEQL HRVAVPSAAS GVNEVVPVVP VQAPEFVRKV TAMMMAGAGD
QLPVSMLPID GTYPSGTTQW EKRNISAFVP HWEPDICIQC GNCSFVCPHA VIRSKFYPQT
LLQSAPENFK SAPISARGFP ETRYTLQIYV EDCTGCALCV EVCPAKSLQQ SGVKAINMKE
KAPVLEQERA NIGFFEQIPV NDRARVDFAS VRGAQFLEPL FEFSGACAGC GETPYVRLLS
QLFGDRLIMA NATGCSSIYG GNLPTTPWTK NGEGRGPAWS NSLFEDNAEF GLGFRLTADK
HLALAHDLAA ALKNEISPAL IDGILDAPQT TESQIRRQRI RVAELKAALL KLDSETARDL
LSVVDHLVRR SVWIMGGDGW AYDIGSGGVD HVLASGRDIN ILVLDTEVYS NTGGQMSKAT
PMGAVAKFAA GGKPLAKKDL ALQAISYGNV YVARIAMGAN PQQTLLALRE AEAYPGPSLV
LAYSHCIAHG INMQHGLKQQ DLAVASGHWP LVRYNPALRQ SDRNPFVLDS PRPHVKLKDY
AFNELRYKML ARQHPAESEH LMTLAQQVVN QKWEIYEEMA SRSGSHFHPD AGVK
//
