ID F5L6C9_CALTT Unreviewed; 158 AA.
AC F5L6C9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Flavodoxin {ECO:0000256|RuleBase:RU367037};
GN ORFNames=CathTA2_1342 {ECO:0000313|EMBL:EGL83129.1};
OS Caldalkalibacillus thermarum (strain TA2.A1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL83129.1, ECO:0000313|Proteomes:UP000010716};
RN [1] {ECO:0000313|EMBL:EGL83129.1, ECO:0000313|Proteomes:UP000010716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL83129.1,
RC ECO:0000313|Proteomes:UP000010716};
RX PubMed=21685297; DOI=10.1128/JB.05035-11;
RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA Cook G.M.;
RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT thermarum strain TA2.A1.";
RL J. Bacteriol. 193:4290-4291(2011).
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|ARBA:ARBA00005267, 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:EGL83129.1}.
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DR EMBL; AFCE01000123; EGL83129.1; -; Genomic_DNA.
DR RefSeq; WP_007504285.1; NZ_AFCE01000123.1.
DR AlphaFoldDB; F5L6C9; -.
DR eggNOG; COG0716; Bacteria.
DR OrthoDB; 9790745at2; -.
DR Proteomes; UP000010716; 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; PTHR42809:SF1; FLAVODOXIN 1; 1.
DR PANTHER; PTHR42809; FLAVODOXIN 2; 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:UP000010716};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367037}.
FT DOMAIN 4..145
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 158 AA; 17498 MW; AF4246EA31ED2713 CRC64;
MYRVVIIYAS MTGNTEAIAM EIARCITNEA QNIQVETKEM EGLDAQVVLD YDGILLGSYT
WGDGELPFEA EDFCDGLANL DLSGKVVACF GSGDHAYPQF CAAVDLLQKQ VEECGACVLP
NGLKIELEPD EEDREQCREF ARLFIQLLFQ EGVDKWAG
//