ID   FLAV_ECOLI              Reviewed;         176 AA.
AC   P61949; P23243;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Flavodoxin 1;
DE   AltName: Full=Flavodoxin A;
GN   Name=fldA; OrderedLocusNames=b0684, JW0671;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RX   PubMed=1999390; DOI=10.1128/jb.173.5.1729-1737.1991;
RA   Osborne C., Chen L.-M., Matthews R.G.;
RT   "Isolation, cloning, mapping, and nucleotide sequencing of the gene
RT   encoding flavodoxin in Escherichia coli.";
RL   J. Bacteriol. 173:1729-1737(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11.
RX   PubMed=7961651; DOI=10.1016/s0021-9258(18)46999-2;
RA   Jenkins C.M., Waterman M.R.;
RT   "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support
RT   bovine cytochrome P450c17 hydroxylase activities.";
RL   J. Biol. Chem. 269:27401-27408(1994).
RN   [6]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [7]
RP   FUNCTION IN COBALT REDUCTION OF COB(II)ALAMIN.
RX   PubMed=9730838; DOI=10.1021/bi9808565;
RA   Jarrett J.T., Hoover D.M., Ludwig M.L., Matthews R.G.;
RT   "The mechanism of adenosylmethionine-dependent activation of methionine
RT   synthase: a rapid kinetic analysis of intermediates in reductive
RT   methylation of Cob(II)alamin enzyme.";
RL   Biochemistry 37:12649-12658(1998).
RN   [8]
RP   STRUCTURE BY NMR.
RX   PubMed=9119004; DOI=10.1111/j.1432-1033.1997.00384.x;
RA   Ponstingl H., Otting G.;
RT   "NMR assignments, secondary structure and hydration of oxidized Escherichia
RT   coli flavodoxin.";
RL   Eur. J. Biochem. 244:384-399(1997).
RN   [9] {ECO:0007744|PDB:1AG9, ECO:0007744|PDB:1AHN}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-176 IN COMPLEX WITH FMN, AND
RP   COFACTOR.
RX   PubMed=9416602; DOI=10.1002/pro.5560061205;
RA   Hoover D.M., Ludwig M.L.;
RT   "A flavodoxin that is required for enzyme activation: the structure of
RT   oxidized flavodoxin from Escherichia coli at 1.8-A resolution.";
RL   Protein Sci. 6:2525-2537(1997).
RN   [10] {ECO:0007744|PDB:2MOK}
RP   STRUCTURE BY NMR IN COMPLEX WITH FMN, COFACTOR, SUBUNIT, AND DOMAIN.
RX   PubMed=25093851; DOI=10.1371/journal.pone.0103936;
RA   Ye Q., Hu Y., Jin C.;
RT   "Conformational dynamics of Escherichia coli flavodoxins in apo- and holo-
RT   states by solution NMR spectroscopy.";
RL   PLoS ONE 9:e103936-e103936(2014).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox enzymes
CC       (Potential). Involved in the reactivation of inactive cob(II)alamin in
CC       methionine synthase. {ECO:0000269|PubMed:9730838, ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:25093851, ECO:0000269|PubMed:9416602};
CC       Note=Binds 1 FMN non-covalently. {ECO:0000269|PubMed:25093851};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25093851}.
CC   -!- INTERACTION:
CC       P61949; P33596: recX; NbExp=3; IntAct=EBI-550021, EBI-1129990;
CC       P61949; P76066: ydaW; NbExp=2; IntAct=EBI-550021, EBI-9142914;
CC   -!- DOMAIN: The structure is significantly stabilized upon cofactor
CC       binding. {ECO:0000269|PubMed:25093851}.
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   EMBL; M59426; AAA23789.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73778.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35333.1; -; Genomic_DNA.
DR   PIR; A37319; A37319.
DR   RefSeq; NP_415210.1; NC_000913.3.
DR   RefSeq; WP_001018618.1; NZ_STEB01000044.1.
DR   PDB; 1AG9; X-ray; 1.80 A; A/B=2-176.
DR   PDB; 1AHN; X-ray; 2.60 A; A=2-176.
DR   PDB; 2MOK; NMR; -; A=1-176.
DR   PDBsum; 1AG9; -.
DR   PDBsum; 1AHN; -.
DR   PDBsum; 2MOK; -.
DR   AlphaFoldDB; P61949; -.
DR   BMRB; P61949; -.
DR   SMR; P61949; -.
DR   BioGRID; 4261909; 12.
DR   BioGRID; 849670; 11.
DR   DIP; DIP-48242N; -.
DR   IntAct; P61949; 29.
DR   STRING; 511145.b0684; -.
DR   DrugBank; DB03247; Flavin mononucleotide.
DR   jPOST; P61949; -.
DR   PaxDb; P61949; -.
DR   PRIDE; P61949; -.
DR   EnsemblBacteria; AAC73778; AAC73778; b0684.
DR   EnsemblBacteria; BAA35333; BAA35333; BAA35333.
DR   GeneID; 67413732; -.
DR   GeneID; 945293; -.
DR   KEGG; ecj:JW0671; -.
DR   KEGG; eco:b0684; -.
DR   PATRIC; fig|1411691.4.peg.1592; -.
DR   EchoBASE; EB0314; -.
DR   eggNOG; COG0716; Bacteria.
DR   HOGENOM; CLU_051402_1_1_6; -.
DR   InParanoid; P61949; -.
DR   OMA; ICGIPTW; -.
DR   PhylomeDB; P61949; -.
DR   BioCyc; EcoCyc:FLAVODOXIN1-MON; -.
DR   BioCyc; MetaCyc:FLAVODOXIN1-MON; -.
DR   EvolutionaryTrace; P61949; -.
DR   PRO; PR:P61949; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; 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   3D-structure; Direct protein sequencing; Electron transport; Flavoprotein;
KW   FMN; Nucleotide-binding; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1999390,
FT                   ECO:0000269|PubMed:7961651"
FT   CHAIN           2..176
FT                   /note="Flavodoxin 1"
FT                   /id="PRO_0000171622"
FT   DOMAIN          4..165
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         10..15
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:1AG9, ECO:0007744|PDB:1AHN,
FT                   ECO:0007744|PDB:2MOK"
FT   BINDING         56..60
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:1AG9, ECO:0007744|PDB:1AHN,
FT                   ECO:0007744|PDB:2MOK"
FT   BINDING         90
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:1AG9, ECO:0007744|PDB:1AHN,
FT                   ECO:0007744|PDB:2MOK"
FT   BINDING         94..99
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:1AG9, ECO:0007744|PDB:1AHN,
FT                   ECO:0007744|PDB:2MOK"
FT   BINDING         147
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:1AG9, ECO:0007744|PDB:1AHN"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   HELIX           14..26
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   STRAND          31..35
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   HELIX           41..45
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   HELIX           64..73
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   TURN            91..96
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   HELIX           100..109
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   TURN            110..113
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:1AHN"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   TURN            150..152
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   HELIX           153..168
FT                   /evidence="ECO:0007829|PDB:1AG9"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:1AG9"
SQ   SEQUENCE   176 AA;  19737 MW;  8878DA1A8EAA55BD CRC64;
     MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA