ID G7LP36_9GAMM Unreviewed; 1177 AA.
AC G7LP36;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN ORFNames=BrE312_3695 {ECO:0000313|EMBL:EHD23045.1};
OS Brenneria sp. EniD312.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD23045.1};
RN [1] {ECO:0000313|EMBL:EHD23045.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD23045.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA Glasner J., Perna N., Woyke T.;
RT "Complete sequence of Brenneria sp. EniD312.";
RL Submitted (JUL-2011) 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=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|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; CM001230; EHD23045.1; -; Genomic_DNA.
DR RefSeq; WP_009114343.1; NZ_CM001230.1.
DR AlphaFoldDB; G7LP36; -.
DR STRING; 598467.BrE312_3695; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_002569_0_0_6; -.
DR Proteomes; UP000002759; 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:0050243; F:pyruvate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000159}; Pyruvate {ECO:0000313|EMBL:EHD23045.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 680..709
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 736..766
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 27
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 60
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 110
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 689
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 692
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 695
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 699
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 745
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 748
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 751
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 755
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 819
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 822
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 824
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 847
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 847
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 965..968
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 994..999
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1074
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 27
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 60
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 110
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 999
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1177 AA; 129101 MW; AB4BEDAF72AB54B5 CRC64;
MITTDGNNTV ASVAWRTNEV IAIYPITPSS TMAEQAAAWS SDGGKNIWGD TPRVVEMQSE
GGAIAAVHGA LQTGSLATTF TSSQGLLLMI PSLYKLAGEL TPFVLHVAAR TVATHALSIF
CDHSDVMAVR QTGCAMLCAS NVQEAQDFAL IAQIASLNSR LPFIHFFDGF RTSHEINKIE
PLSDDALRRL LPRQAIDAHR ERALTPEHPV IRGTASNPDT FFQAREAANP WYNAACRHVE
QAMNDFADVT GRQYRPFEYY GHPEATRVIV LMGSGVGTVE EVVDTLLTRG EKVGVVKIRL
YRPFSARHLL AVIPQTAQNI AVLDRTKEPG ALAEPLYLDV MTSLAEAFTN GERPQMPRVI
GGRYGLSSKE FTPQCVQAVF NELAIANPRS RFTVGIYDDV TNLSLPLPIE HLPGSASLEA
LFYGLGSDGT VSAAKNSIKI VGDATPMFVQ GYFVYDSKKA GSLTVSHMRV GPHPINSAYL
IDQADFVACH QWQFIDKYSM VERLKPGGVF LINAPYASDD LWHRLPQEVQ AGLNQRQARV
YCINAAKIAR ECQLGARINT VMQMAFFHLS QILPGEEAVE KLRTAIAKSY GSKGQELVER
NWRALNATLE ALAAVPLEAV NAHSPQRPPV VSDAAPDFVK TVTAAMLAGL GDTLPVSALP
PDGTWPTGTT KWEKRNIAEA IPLWQPQLCT QCNHCVAACP HSAIRAKVVP AEAMEYAPAS
LQSLDVKARD MRGQKYVLQV APEDCTGCNL CVEVCPAKDR QDPTIKAINM ESRLDNLAVE
KEHFDFFMTL PEIDRSRLER IDIRTSQLIS PLFEYSGACS GCGETPYIKL LTQLYGDRLL
VANATGCSSI YGGNLPTTPW TTDANGRGPA WANSLFEDNA EFGLGFRLSV DQHRQRAVRL
LHDLAPRLPA DLVAALQEEA IAPELRRQQI EQLRTLLATI GGDKAAALAA AADHLVDKSI
WLIGGDGWAY DIGYGGLDHV MSLSENVNVL VLDTQCYSNT GGQQSKATPL GAVTKFGEKG
KRKARKDLGI SVMMYGHVYV AQISLGAQLN QTVKAIQEAE AWPGPSLIIA YSPCEEHGYD
LAFSHDQMRQ LTATGFWPLY RFDPRRTEEG KPALVTDSRP PSTSLSETLL HEQRFRRLNS
LMPEETALLY EEAEVDLRRR YDFLTMMAGK AEKNPQE
//