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Database: UniProt
Entry: A0A0A8B5W0_9ACTN
LinkDB: A0A0A8B5W0_9ACTN
Original site: A0A0A8B5W0_9ACTN 
ID   A0A0A8B5W0_9ACTN        Unreviewed;       139 AA.
AC   A0A0A8B5W0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Flavodoxin {ECO:0000256|RuleBase:RU367037};
GN   ORFNames=JI75_02970 {ECO:0000313|EMBL:AJC12739.1};
OS   Berryella intestinalis.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Berryella.
OX   NCBI_TaxID=1531429 {ECO:0000313|EMBL:AJC12739.1, ECO:0000313|Proteomes:UP000031121};
RN   [1] {ECO:0000313|Proteomes:UP000031121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-1-3 {ECO:0000313|Proteomes:UP000031121};
RA   Looft T., Bayles D.O., Stanton T.B.;
RT   "Coriobacteriaceae sp. complete genome.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AJC12739.1, ECO:0000313|Proteomes:UP000031121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-1-3 {ECO:0000313|EMBL:AJC12739.1,
RC   ECO:0000313|Proteomes:UP000031121};
RX   PubMed=26450725;
RA   Looft T., Bayles D.O., Alt D.P., Stanton T.B.;
RT   "Complete Genome Sequence of Coriobacteriaceae Strain 68-1-3, a Novel
RT   Mucus-Degrading Isolate from the Swine Intestinal Tract.";
RL   Genome Announc. 3:e01143-15(2015).
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}.
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DR   EMBL; CP009302; AJC12739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8B5W0; -.
DR   STRING; 1531429.JI75_02970; -.
DR   KEGG; cbac:JI75_02970; -.
DR   HOGENOM; CLU_051402_4_3_11; -.
DR   Proteomes; UP000031121; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
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   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:UP000031121};
KW   Transport {ECO:0000256|RuleBase:RU367037}.
FT   DOMAIN          4..139
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   139 AA;  14953 MW;  85E1F27A899718FD CRC64;
     MSNVAVVFWS GTGNTEAMAD LVAQGASAKG AKVSIIQASD FGADRLDGYD AVAFGCPAMG
     DEELEDTEFL PMYDEVEPLL GDRKVVLFGS YDWNDGEWME LWEQRAEAAG VNVVDSLIAK
     DYPDDEASAE CMRVGALLA
//
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