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Database: UniProt
Entry: F6INX3_9SPHN
LinkDB: F6INX3_9SPHN
Original site: F6INX3_9SPHN 
ID   F6INX3_9SPHN            Unreviewed;      1201 AA.
AC   F6INX3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   ORFNames=PP1Y_AT22962 {ECO:0000313|EMBL:CCA93125.1};
OS   Novosphingobium sp. PP1Y.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA93125.1, ECO:0000313|Proteomes:UP000009242};
RN   [1] {ECO:0000313|EMBL:CCA93125.1, ECO:0000313|Proteomes:UP000009242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX   PubMed=21685292; DOI=10.1128/JB.05349-11;
RA   D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA   Paolella G., Di Donato A., Salvatore F.;
RT   "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT   strain PP1Y.";
RL   J. Bacteriol. 193:4296-4296(2011).
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; FR856862; CCA93125.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6INX3; -.
DR   KEGG; npp:PP1Y_AT22962; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1013; Bacteria.
DR   eggNOG; COG1014; Bacteria.
DR   eggNOG; COG1145; Bacteria.
DR   HOGENOM; CLU_002569_0_0_5; -.
DR   OrthoDB; 9800445at2; -.
DR   Proteomes; UP000009242; 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   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   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR033412; PFOR_II.
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:CCA93125.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009242};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN          678..707
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          734..764
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         24
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         57
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         107
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         687
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         690
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         693
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         697
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         743
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         746
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         749
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="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         817
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         820
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="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         845
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         845
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         967..970
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         996..1001
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         1076
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   SITE            24
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            57
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            107
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            1001
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ   SEQUENCE   1201 AA;  131096 MW;  BA40030379B24A9D CRC64;
     MDGNAAVAHV AYRVNDVCAI FPITPASPMA ELADEWSAEG RTNLWGAVPI VQEMQAEGGA
     VGAVHGSLQA GALTTTFTAS QGLLLMMPNM FKIAGELTPC VFHVAARSIA TQALSIFGDH
     SDVMAVRGTG FALLGAASVQ EAHDLALVAQ AATLESRVPF LHFMDGFRTS HEVNTVTMLS
     NDDIRAMIDD ELVRAHRQRA LSPERPVTRG TAHNPDTFFQ ARETVNPFYL ATPAIVQRAM
     DRFAKLTGRH YQLFRYDGHV EPERVVVVMG SAAETLRATI AHLTAQGERV GFIQVLLYRP
     WSAEDFLDAL PASVRKVAVL DRTKEPGAPA EPLCLDVAQT LADAFARGAR KDLPLVVGGR
     YGLSSKDFTP AMAKAVFDHL ESNDPRTCFT IGINDDVCGT SLPVETGFEI EPPGTTRALF
     FGLGADGTVG ANKNSVKILA EDPERHAQGY FVYDSHKSGA ETVSHLRFGN APIAAPYLLS
     SADFIGVHKF EFLDKLDVLR HAREGATLLI NAPYDPAKLW DHLRRPVQQH ILDKHLRLFV
     IDASGVAQRL GLGPRVNTIL QTCFFAISGV LPREEGVRRI RAAIEKTYGD KGRAILEKNF
     AAVDSALDHL HEVTVPSSVT STEELHVFVP PDAPDQMRRI AALQFAGRGD EIPVSAIPVD
     GSYVGGTTQY EKRNIAFEVP VWEPDLCIQC GQCSIVCPHS VIRAKSYDGA LLEGAPEGFL
     SAPVNARGYP DKNFTLQIAV EDCTGCGLCV DHCPAHDPLD ASVKAINLSE RQPQIEPGRR
     NLAFFDTLPE HARQDVDLHL SRGLQFVRPL FEFSGACAGC GETPYLKLLS QLFGDRLQIA
     NATGCTSIYG GNLPALPWRS GPDGRGPAWN NSLFEDNAEF GYGMRLAVDQ QVAMAYALVR
     TLADRIGPRL AAQILDAPQR TDSEIVAQRT RVEDLRRALA DATDGLARNL LALSEYLVRR
     SLWIVGGDGW AYDIGAGGLD HVLAQPRNVN VLVLDTEVYS NTGGQASKAT PVGAAAKFAA
     AGKRTPRKDL ALQAIASGYV YVAQIALAGS PEQTIQALRD AEEYEGPSLI LAYSQCIAHG
     LKLNLRDGMK QQRRAVASGY WPLFRYDPRM RQAGMNPFRL DSTRPRLPLE DFAYQELRYR
     ILTHTRPEEA RVLLRQAQAA VDERYRLYED IAARDGTRFH PFWQEESVAP HDGNETGEAA
     Q
//
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