FLAV_AQUAE
ID FLAV_AQUAE Reviewed; 185 AA.
AC O67866;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Flavodoxin;
GN Name=fldA; Synonyms=floX; OrderedLocusNames=aq_2096;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07825.1; -; Genomic_DNA.
DR PIR; F70479; F70479.
DR RefSeq; NP_214435.1; NC_000918.1.
DR RefSeq; WP_010881371.1; NC_000918.1.
DR PDB; 2ARK; X-ray; 2.40 A; A/B/C/D/E/F=1-185.
DR PDBsum; 2ARK; -.
DR AlphaFoldDB; O67866; -.
DR SMR; O67866; -.
DR STRING; 224324.aq_2096; -.
DR EnsemblBacteria; AAC07825; AAC07825; aq_2096.
DR KEGG; aae:aq_2096; -.
DR eggNOG; COG0655; Bacteria.
DR HOGENOM; CLU_051402_2_0_0; -.
DR InParanoid; O67866; -.
DR OMA; CTTATVH; -.
DR OrthoDB; 796211at2; -.
DR EvolutionaryTrace; O67866; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Flavoprotein; FMN; Reference proteome;
KW Transport.
FT CHAIN 1..185
FT /note="Flavodoxin"
FT /id="PRO_0000171602"
FT DOMAIN 4..159
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2ARK"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:2ARK"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2ARK"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:2ARK"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2ARK"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2ARK"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:2ARK"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2ARK"
FT STRAND 130..141
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 145..165
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:2ARK"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2ARK"
SQ SEQUENCE 185 AA; 20444 MW; 7C138666D5B89281 CRC64;
MGKVLVIYDT RTGNTKKMAE LVAEGARSLE GTEVRLKHVD EATKEDVLWA DGLAVGSPTN
MGLVSWKMKR FFDDVLGDLW GEIDGKIACA FSSSGGWGGG NEVACMSILT MLMNFGFLVF
GVTDYVGKKF TLHYGAVVAG EPRSEEEKEA CRRLGRRLAE WVAIFVDGRK ELLEKIRKDP
ARFVD