ID Q32BV8_SHIDS Unreviewed; 173 AA.
AC Q32BV8;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN Name=fldB {ECO:0000313|EMBL:ABB63197.1};
GN OrderedLocusNames=SDY_3187 {ECO:0000313|EMBL:ABB63197.1};
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB63197.1, ECO:0000313|Proteomes:UP000002716};
RN [1] {ECO:0000313|EMBL:ABB63197.1, ECO:0000313|Proteomes:UP000002716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB63197.1,
RC ECO:0000313|Proteomes:UP000002716};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC {ECO:0000256|ARBA:ARBA00003297, ECO:0000256|PIRNR:PIRNR038996}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR038996};
CC -!- SIMILARITY: Belongs to the flavodoxin family.
CC {ECO:0000256|ARBA:ARBA00005267, ECO:0000256|PIRNR:PIRNR038996}.
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DR EMBL; CP000034; ABB63197.1; -; Genomic_DNA.
DR RefSeq; WP_001055874.1; NC_007606.1.
DR RefSeq; YP_404688.1; NC_007606.1.
DR AlphaFoldDB; Q32BV8; -.
DR SMR; Q32BV8; -.
DR STRING; 300267.SDY_3187; -.
DR EnsemblBacteria; ABB63197; ABB63197; SDY_3187.
DR GeneID; 75205268; -.
DR KEGG; sdy:SDY_3187; -.
DR PATRIC; fig|300267.13.peg.3809; -.
DR HOGENOM; CLU_051402_1_0_6; -.
DR Proteomes; UP000002716; 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; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR010086; Flavodoxin_lc.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR NCBIfam; TIGR01752; flav_long; 1.
DR PANTHER; PTHR42809; FLAVODOXIN 2; 1.
DR PANTHER; PTHR42809:SF3; FLAVODOXIN 2; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR PIRSF; PIRSF038996; FldA; 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|PIRNR:PIRNR038996};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR038996};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR038996};
KW Reference proteome {ECO:0000313|Proteomes:UP000002716};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR038996}.
FT DOMAIN 3..165
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 173 AA; 19700 MW; 89338715D106A68C CRC64;
MNMGLFYGSS TCYTEMAAEK IRDIIGPELV TLHNLKDDSP KLMEQYDVLI LGIPTWDFGE
IQEDWEAVWD QLDDLNLEGK IVALYGLGDQ LGYGEWFLDA LGMLHDKLST KGVKFVGYWP
TEGYEFTSPK PVIADGQLFV GLALDETNQY DLSDERIQSW CEQILNEMAE HYA
//
