ID B0S157_FINM2 Unreviewed; 139 AA.
AC B0S157;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Flavodoxin {ECO:0000256|RuleBase:RU367037};
GN OrderedLocusNames=FMG_0679 {ECO:0000313|EMBL:BAG08097.1};
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG08097.1, ECO:0000313|Proteomes:UP000001319};
RN [1] {ECO:0000313|EMBL:BAG08097.1, ECO:0000313|Proteomes:UP000001319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC {ECO:0000313|Proteomes:UP000001319};
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008971; BAG08097.1; -; Genomic_DNA.
DR RefSeq; WP_012290563.1; NC_010376.1.
DR AlphaFoldDB; B0S157; -.
DR STRING; 334413.FMG_0679; -.
DR KEGG; fma:FMG_0679; -.
DR eggNOG; COG0716; Bacteria.
DR HOGENOM; CLU_051402_4_3_9; -.
DR Proteomes; UP000001319; Chromosome.
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 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:UP000001319};
KW Transport {ECO:0000256|RuleBase:RU367037}.
FT DOMAIN 3..138
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 139 AA; 16029 MW; 63CD8BCFD305CB35 CRC64;
MNLLILYWSQ TGNTEKMAQI IKDECESKGS KVEMVFSDDY QNCNIDNFDV IAFGCPAMGD
EELEDTSFEP MFSDLENKLN DKKIALFGSY EWNNGEWMGF WKERCDKNNL NVIDTVICYD
APDENSTNDI KTFADNLLK
//