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Database: UniProt
Entry: W2BXJ8_9FIRM
LinkDB: W2BXJ8_9FIRM
Original site: W2BXJ8_9FIRM 
ID   W2BXJ8_9FIRM            Unreviewed;       140 AA.
AC   W2BXJ8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Flavodoxin {ECO:0000256|RuleBase:RU367037};
GN   ORFNames=HMPREF0378_1203 {ECO:0000313|EMBL:ETJ99619.1};
OS   Eubacterium nodatum ATCC 33099.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=1161902 {ECO:0000313|EMBL:ETJ99619.1, ECO:0000313|Proteomes:UP000018868};
RN   [1] {ECO:0000313|EMBL:ETJ99619.1, ECO:0000313|Proteomes:UP000018868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33099 {ECO:0000313|EMBL:ETJ99619.1,
RC   ECO:0000313|Proteomes:UP000018868};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC       {ECO:0000256|RuleBase:RU367037}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|RuleBase:RU367037};
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC       {ECO:0000256|RuleBase:RU367037}.
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:ETJ99619.1}.
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DR   EMBL; AZKM01000018; ETJ99619.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2BXJ8; -.
DR   STRING; 1161902.HMPREF0378_1203; -.
DR   PATRIC; fig|1161902.3.peg.829; -.
DR   eggNOG; COG0716; Bacteria.
DR   OrthoDB; 9790745at2; -.
DR   Proteomes; UP000018868; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   NCBIfam; TIGR01753; flav_short; 1.
DR   PANTHER; PTHR43717; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR   PANTHER; PTHR43717:SF1; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU367037};
KW   Flavoprotein {ECO:0000256|RuleBase:RU367037};
KW   FMN {ECO:0000256|RuleBase:RU367037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018868};
KW   Transport {ECO:0000256|RuleBase:RU367037}.
FT   DOMAIN          3..139
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   140 AA;  14931 MW;  13B25270528DAFF9 CRC64;
     MKVAVVYWSG TGNTEMMAQA VAEGAKEKGA EVSIFTPEEF NAGMTADFDS IALGCAAMGD
     EVLEEGEFQP MYDDIKDSLK DKKVALFGSY GWGDGQWIRD WEDDCTSAGI KLAAGSVMCN
     YAPDDEGTAE CKELGASLAV
//
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