ID A0A1H3HVQ6_9BACI Unreviewed; 1180 AA.
AC A0A1H3HVQ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate-ferredoxin/flavodoxin oxidoreductase {ECO:0000313|EMBL:SDY19601.1};
GN ORFNames=SAMN05421736_101631 {ECO:0000313|EMBL:SDY19601.1};
OS Evansella caseinilytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella.
OX NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDY19601.1, ECO:0000313|Proteomes:UP000198935};
RN [1] {ECO:0000313|Proteomes:UP000198935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP {ECO:0000313|Proteomes:UP000198935};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNPI01000001; SDY19601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3HVQ6; -.
DR STRING; 1503961.SAMN05421736_101631; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000198935; 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; 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:SDY19601.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198935};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 682..711
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 735..766
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 691
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 694
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="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 701
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 744
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 754
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 811
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 814
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 839
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 1073
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 28
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 61
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 111
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 998
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1180 AA; 129711 MW; 19E93BC7EE18624D CRC64;
MKKIIDGNEA AAWMSYAFTE AAVLYPITPA TGMAEKVEKW AAAGRTNAFH HSIKIIPMQS
EAGVAGTLHG LLKAGTLAAA YTCSQGLLLM LPTIYKLVGE LLPAVIHVAA RSVASSALSI
FGDHSDVMAV RQTGAVMLSA ASVQEAALFS AVAHLTAVEG SLPVIHFFDG FNTSHELQKI
EVPDYKVIKK RMDQAAYLAF KDKAISNEQP RAYGSSQTPD IFFQQLEAAN AVHTAIPQIV
QSCLEELNPL FQTNCSIVDY DGSNMAEVVI VIMGSVSGTV GQVVYEQNEA GNRCGVITIH
LYRPFPTAFF LKKLPASVKT IVVLDRTKER GSQGEPLLLD VQSACYELPE RPVIIGGRYG
LGSKDVTPDQ IRGVLHESRK ARPKSRFTIG IIDDVTHLSL LPKGNKDLTG DTIYQVKVWG
RGSDGAVSCS RQTVKIVGQE TDLEVQGQFW HDAKKTGGLT VSQLRFGREA IRSAYKVQNS
DFISCYDERY LKQYNVLAGL RENGIFLLNS SCPDAPGDAI SVETKRFLAR KNIQFYTINA
GKIANQFNLG PYINTIMQTL FFYLTDLLPF EKAIQRLKEE IKKAYGEHDP AMVAANHRAM
ELAVANVMKV DVPERWNHFI ADASFKRKPA EGARTFQTLI QQPLQKQEGN TISVGDLLRS
GMIDGSLPLG TSAMEKRGIA EQLPAWDEEF CLQCNLCAAV CPHAAIRPFL MNAERSDAPP
GFSTIPASGV ESAMFRIQIS PDDCTGCSLC AEACPAAPSA LTMKAAGRWK EDENELWSYA
LQNGINDHPF RQTSLKGSQF NRPLLEFSGA CAGCGETPYV KLLTQLFGDR IVIANATGCS
SIWGCSLPSV PYTTNGDGCG PVWGNSLLEN NAEYGYGMKL GLDVIQNHFL EEAEACLRQE
KYSPLFRKTL EEWLEAYRLG RHTRKTAHQL IRALVNEKQT HPDLEPLYRL RRHLTARSQW
IVGGDGWAYD IGFGGIDHIV AQGSNVNILV LDNEGYANTG GQASKAAPAA SRVKFSSNGS
NSSKKDFGLM MMSYGDVYVA QICMSADPNQ TIAALTEAEA YPGPAIVIAY CPCVLHGMNS
RSMLTEGKKA VECGYWTLYR YDPRKKKKGR SPMRIDSSPP KWSLFQDFLQ GEARFSSVCR
FNKKTGEALL AQNEANAKRR YSNYRMLSEM KMDENDTHKV
//
