ID D2TS19_CITRI Unreviewed; 173 AA.
AC D2TS19;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Flavodoxin {ECO:0000256|PIRNR:PIRNR038996};
GN Name=fldB {ECO:0000313|EMBL:CBG91619.1};
GN OrderedLocusNames=ROD_49381 {ECO:0000313|EMBL:CBG91619.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91619.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91619.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91619.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG91619.1; -; Genomic_DNA.
DR RefSeq; WP_012908781.1; NC_013716.1.
DR AlphaFoldDB; D2TS19; -.
DR STRING; 637910.ROD_49381; -.
DR KEGG; cro:ROD_49381; -.
DR eggNOG; COG0716; Bacteria.
DR HOGENOM; CLU_051402_1_0_6; -.
DR OrthoDB; 359268at2; -.
DR Proteomes; UP000001889; 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 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; 19610 MW; CD0439F5CBDC5F6C CRC64;
MKIGLFYGSS TCYTEMAAEK IRDIIGPELV TLHNLKDDAP ALMEQYDVLI LGIPTWDFGE
IQEDWEAVWD QLDELNLEGK IVALYGMGDQ LGYGEWFLDA LGMLHDKLST KGVRFVGYWP
TEGYEFTSPK PVIADGQLFV GLALDETNQY DLSDERIQAW CEQILGEMAE HYA
//
