ID B2KCW5_ELUMP Unreviewed; 1185 AA.
AC B2KCW5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Pyruvate:ferredoxin oxidoreductase {ECO:0000313|EMBL:ACC98361.1};
GN OrderedLocusNames=Emin_0806 {ECO:0000313|EMBL:ACC98361.1};
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC98361.1, ECO:0000313|Proteomes:UP000001029};
RN [1] {ECO:0000313|EMBL:ACC98361.1, ECO:0000313|Proteomes:UP000001029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191 {ECO:0000313|EMBL:ACC98361.1,
RC ECO:0000313|Proteomes:UP000001029};
RX PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC98361.1; -; Genomic_DNA.
DR RefSeq; WP_012414976.1; NC_010644.1.
DR AlphaFoldDB; B2KCW5; -.
DR STRING; 445932.Emin_0806; -.
DR KEGG; emi:Emin_0806; -.
DR HOGENOM; CLU_002569_0_0_0; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000001029; 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; 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; 2.
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:ACC98361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001029};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 683..712
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 738..768
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 30
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 63
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 113
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
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 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 823
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 825
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 848
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 848
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 972..975
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1001..1006
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1081
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 30
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 63
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 113
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 1006
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1185 AA; 128056 MW; 14EB93ABFE2B50CA CRC64;
MAKLVAMDGN SAVAHVAHAT NEVIAIYPIT PSSNMGEISD LKSAKGEKNI WGNTPIVSEL
QSEGGASGTV HGALSAGALT TTFTASQGLL LMIPNMYKIS GELTPTVFHV SARAIATHAL
SIFGDHSDVM AVRQTGWAML ASANPQEAMD FALISQAATL EARVPFLHFF DGFRTSHELN
MVDPLTKEQM LEMLDADLIA KHRTTALNPE HPTIRGTAQN PDVYFQGREA VNKFFTATPA
IVKKYMEKFE KVAGRKYDLF EYVGDADADK LVIIMASGAD VAETAVECLK GSKVGVLKVR
LFRPFSIEHF VNAIPKTVKK IAVMDRTKEP GALGEPLFLD VCSAFLTEEG RKAFPVTPII
VGGRYGIGSK EFTPGMVKAV FDNLAKDQPK KSFVVGIIDD LTDSSLPNSI DCDSLGTSDT
FGAMFFGLGS DGTVGANKNT MKIISEKSDN YSQGYFVYDS KKAGSMTTSH IRFGKKVIKA
PYLIEKADFI ACHMFSFLEK YDVLSKLKIG GTFLLNAPYP ADQVWDHIPA EVQQQIIDKN
AKFYAIDASE IALKTGMGAR TNTIMQTAFF AISDVIETAK AIEAIKEAIK KTYSKKGEEI
VNKNYAAVDA ALDGLKEVKY DKKVTSKLNV KPSVPSSAPK MVKEVLGEMI AFRGDSLPTS
AMPEGGIFPT ATTQYEKRNI ALLCPQWDPE VCIQCGICSL VCPHAAIRMK AYSADQLDNA
PKTFKSADGK ADLAGNKVTI QVAVEDCTGC GACVFNCPAK NKTNPERKAI NMTHQLPLRD
TEIDNFAFFL GLKSAEVKTK KESIKGSQLQ TPLFEFSGAC AGCGETPYVK LLTQLHGDHI
TIANATGCSS IYGGNLPTTP YCKRDDGKGP AWANSLFEDN AEFGLGIRLA YDQLKSDAEA
LLKDVAANVK EVEPLAKEIL EAKQVSTQDV DAQRARVAAL KEVLAKQKCA HCARLASIAD
YLIKKSVWIL GGDGWAYDIG YGGLDHVLAS GKNVKVLVMD TEVYSNTGGQ MSKATPMGAV
AQFAAGGKTQ PKKDLGMISM TYGNIYVAQI SMGANMYQAV QALAEAEAYD GPAIVIAYAH
CIAHGIDMSK GMGEGKKAVQ SGRWQLYRFN PDLKAQGKNP LTLDSGAPTI DVADFMGGEN
RFKTLAKANP EVAAKLLNLA KAEYDWRRSV YEQLANFKCD VKKAD
//
