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Database: UniProt
Entry: A0A0J1GAD2_9FIRM
LinkDB: A0A0J1GAD2_9FIRM
Original site: A0A0J1GAD2_9FIRM 
ID   A0A0J1GAD2_9FIRM        Unreviewed;       154 AA.
AC   A0A0J1GAD2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Flavodoxin {ECO:0000256|RuleBase:RU367037};
GN   ORFNames=RHS_1925 {ECO:0000313|EMBL:KLU72298.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU72298.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU72298.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU72298.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
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:KLU72298.1}.
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DR   EMBL; JNGB01000016; KLU72298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1GAD2; -.
DR   PATRIC; fig|1504536.3.peg.1887; -.
DR   Proteomes; UP000036477; 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:UP000036477};
KW   Transport {ECO:0000256|RuleBase:RU367037}.
FT   DOMAIN          15..152
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   154 AA;  17033 MW;  8296E0AF4FA118BF CRC64;
     MENADRKKEN IMKTIKVVYW SGTGNTQAMA QAIAEGVEKG EAKADLLDVD TIKADDLKDD
     SIFAMGCPAM GDEVLEEGSM EPFMEELESN LSGKQVALFG SYGWGDGQWM RDWEERVTEK
     GGKLVEGKGL MCCEEPDDQV LEDCRKLGEK LAKL
//
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