ID   FLAW_AZOVD              Reviewed;         174 AA.
AC   P52964; C1DHX2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Flavodoxin 1 {ECO:0000303|PubMed:8694750};
DE   AltName: Full=AvFld 1 {ECO:0000303|PubMed:8694750};
GN   OrderedLocusNames=Avin_45950 {ECO:0000312|EMBL:ACO80705.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21, MASS SPECTROMETRY, FUNCTION, COFACTOR, INDUCTION,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=OP / UW136;
RX   PubMed=8694750; DOI=10.1042/bj3170103;
RA   Gangeswaran R., Eady R.R.;
RT   "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in
RT   electron donation to purified assimilatory nitrate reductase.";
RL   Biochem. J. 317:103-108(1996).
CC   -!- FUNCTION: Flavodoxins are low-potential electron donors to a number of
CC       redox enzymes. AvFld 1 is able to donate electrons to the assimilatory
CC       nitrate reductase of A.vinelandii to catalyze the reduction of nitrate
CC       to nitrite. {ECO:0000269|PubMed:8694750}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:8694750};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is -330 mV. It is the mid-point potential of the
CC         semiquinone/hydroquinone redox couple (SQ/HQ) of AvFld 1.
CC         {ECO:0000269|PubMed:8694750};
CC   -!- INDUCTION: Is the predominant flavodoxin expressed when A.vinelandii is
CC       grown on nitrate as nitrogen source. {ECO:0000269|PubMed:8694750}.
CC   -!- MASS SPECTROMETRY: Mass=19430; Mass_error=3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8694750};
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   EMBL; CP001157; ACO80705.1; -; Genomic_DNA.
DR   RefSeq; WP_012703069.1; NC_012560.1.
DR   AlphaFoldDB; P52964; -.
DR   SMR; P52964; -.
DR   EnsemblBacteria; ACO80705; ACO80705; Avin_45950.
DR   KEGG; avn:Avin_45950; -.
DR   eggNOG; COG0716; Bacteria.
DR   HOGENOM; CLU_051402_1_0_6; -.
DR   OMA; ILGISTW; -.
DR   OrthoDB; 1961680at2; -.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
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   Pfam; PF00258; Flavodoxin_1; 1.
DR   PIRSF; PIRSF038996; FldA; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Flavoprotein; FMN;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8694750"
FT   CHAIN           2..174
FT                   /note="Flavodoxin 1"
FT                   /id="PRO_0000171606"
FT   DOMAIN          4..168
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         10..14
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         89..122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
SQ   SEQUENCE   174 AA;  19559 MW;  8B53CA5921BAB98F CRC64;
     MSRIGIFYGS SSGVTGKVAE KLAELLGEER CDLYNMEEDF VDFDDMLKYD HLLFGCSTWG
     SGEVQNDWRD PLLELDNEKP DFSGKTIALF GAGDYVSHGE QFVSALGVLY DKFKARGAAL
     VGSFPTDGYT YEYSFAVRDG KFVGLPFDKI NEVDKTDERL ERWIAVLQEE FLPA