ID G1W9S4_9BACT Unreviewed; 1195 AA.
AC G1W9S4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Pyruvate:ferredoxin oxidoreductase {ECO:0000313|EMBL:EGV34242.1};
GN ORFNames=HMPREF9431_00575 {ECO:0000313|EMBL:EGV34242.1};
OS Segatella oulorum F0390.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV34242.1, ECO:0000313|Proteomes:UP000005141};
RN [1] {ECO:0000313|EMBL:EGV34242.1, ECO:0000313|Proteomes:UP000005141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0390 {ECO:0000313|EMBL:EGV34242.1,
RC ECO:0000313|Proteomes:UP000005141};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella oulorum F0390.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGV34242.1}.
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DR EMBL; ADGI01000018; EGV34242.1; -; Genomic_DNA.
DR AlphaFoldDB; G1W9S4; -.
DR PATRIC; fig|702438.4.peg.593; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_002569_0_0_10; -.
DR OrthoDB; 9808559at2; -.
DR Proteomes; UP000005141; Unassembled WGS sequence.
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; 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:EGV34242.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005141};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 683..713
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 738..758
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
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 698
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 702
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 747
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 750
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 757
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 821
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="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 849
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 1084
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 33
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 66
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 116
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 1009
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1195 AA; 132011 MW; 7148E6D37E857AF7 CRC64;
MAKEKKFITC DGNTAAAHIS YMFTEVAAIY PITPSSPMAE HVDEWSAKGR KNLFGQTVSI
QEMESEGGAA GAVHGSLQAG ALTSTYTASQ GLLLMIPNMY KIAGELLPCV FNVSARTLAS
HSLCIFGDHQ DVMACRQTGF AMFCSGSVQE VMDLSAVPHL ASLESSVPFV NFFDGFRTSH
EYHKIEEMDM EDIRPLVKQE FIKRFRDRAL TPERPVTRGT AENPETFFTH REASNQYYDR
IPGIVEKYLG EISKITGREY HLFNYYGAKD AENIIILMGS ATEPAREAID YLVKQGKKVG
MVAVHLYRPF SVEAIRKAIP ETVKRIAVLD RTKEPGAEGE PLYLDVKSAL YEDPRKPLIV
GGRYGLGSSD TTPAKIISVF NNLELPMPKN HFTVGIVDDV TFTSLPEVEE IPLGGEGLYE
AKFYGLGADG TVGANKNSVQ IIGNNTNKYC QAYFSYDSKK SGGFTCSHLR FGDEPIHSAY
QVNTPNFVAC HVQAYLHMYD VTRGLRDNGT FLLNTIFEGE ELVNFIPNKV KAYFAKHNIK
VYYINATKIA QEIGLGNRTN TILQSAFFRI TKVIPTELAV EQMKAFIVKS YGKKGQDVVD
KNYAAVDRGG EYKELAIDPA WAKLPADEDN DGDVPAFIKE IVRPINAQSG DLLKVSDFVK
NDTVDGTWKN GTAAFEKRGV AAFVPVWNAD NCIQCNKCAY CCPHATIRPF VLDDNEKAGF
EGMTMDILAP KQLKGMQFRI QVDVLDCLGC GNCADVCPGK KGEKALVMAP FNVDDPNMKK
EEANWEYMVK HVKSKQDLVD IKQSPKNSQF AQPLFEFSGA CSGCGETPYV KLVSQLFGDR
EMIANATGCS SIYSASIPST PYTTNEKGQG PAFDNSLFED FCEFGLGMAM GNKKMRERIT
VLLNNLIADD KTAADFKSAA QNWIDNKNDA NGSKVAAAAL KPFIEKGAAA GCDVCKELQT
LDHYLVKRSQ WIIGGDGASY DIGYGGLDHV LSTGEDVNIL VLDTEVYSNT GGQSSKSTPL
GAIAQFAAQG KRIRKKDLGL MQTTYGYVYV AQVAMGADNN QTLKAIREAE AYPGPSLVIA
YSPCINHGIK GTKNMKRNMG RSQNEEKLAV DCGYWHLWRY DPRLADEGKN PFQLDSKAPN
FADFREFLMG EVRYSSVAKA YPAEAEELFS EAEKMAKLRY QTYVRKSKED WSEEA
//
