ID A0A0F2JNU7_9FIRM Unreviewed; 532 AA.
AC A0A0F2JNU7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:KJR49100.1};
GN ORFNames=UF75_0615 {ECO:0000313|EMBL:KJR49100.1};
OS Desulfosporosinus sp. I2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR49100.1, ECO:0000313|Proteomes:UP000033442};
RN [1] {ECO:0000313|EMBL:KJR49100.1, ECO:0000313|Proteomes:UP000033442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I2 {ECO:0000313|EMBL:KJR49100.1,
RC ECO:0000313|Proteomes:UP000033442};
RA Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V., Ravin N.V.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJR49100.1}.
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DR EMBL; JYNH01000005; KJR49100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2JNU7; -.
DR PATRIC; fig|1617025.3.peg.632; -.
DR Proteomes; UP000033442; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd03377; TPP_PFOR_PNO; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
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; PF02775; TPP_enzyme_C; 1.
DR SMART; SM00890; EKR; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyruvate {ECO:0000313|EMBL:KJR49100.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033442}.
FT DOMAIN 37..66
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 93..124
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 532 AA; 58780 MW; 0EEE2C72E5C9CF0D CRC64;
MARHDGEDLP TSAFVGVEDG TFPLSTTRYE KRGIAVYLPE WQIDQCIQCN QCAYVCPHAT
IRPFLLDDSE LEKAPDTFKT KKPIGKGLEG YHYRIQVTPL DCTGCANCAD VCPAPGKAIV
MKPADHEIEM ESENWEYAIK NVTEKRQLMD VKTLKGSQFA RPLLEFHGAC PGCGETPYAR
LITQLYGDRM LIANATGCSS IWGGSAPSIP YTVNAEGKGP AWMSPLFEDN AEFGYGIYLG
SKQIRAKLAQ LMQQGLESTI GENLKEAFRE WLENMEDGEG SKRASARVLE AMSKEDAAGN
PIVREIKGKK DYLIKPSVWI FGGDGFAYDI GYNGIDHVIA SGDDVNILVM DTEVYSNTGG
QASKATQTAA IAKFAAAGKK VRKKDLGLIA TTYGYVYVAQ IAMGANMNQT IKAIAEAESY
RGPSIIIAYA TCVNHGIKSG MGTSILEQKK AVEAGYWHLW RHDPRLKEQG KNPFVLDSKE
PSASFQDFLK GEIRYSSLMN VFPEVAQEMF DEAEGHAREK YQTLKRYAEM QY
//
