ID   FLAV_CLOBE              Reviewed;         138 AA.
AC   P00322;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Flavodoxin;
OS   Clostridium beijerinckii (Clostridium MP).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1520;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4843142; DOI=10.1016/s0021-9258(19)42430-7;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G.;
RT   "The amino acid sequence of the Clostridium MP flavodoxin.";
RL   J. Biol. Chem. 249:4393-4396(1974).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF OXIDIZED FORM.
RX   PubMed=4843141; DOI=10.1016/s0021-9258(19)42429-0;
RA   Burnett R.M., Darling G.D., Kendall D.S., Lequesne M.E., Mayhew S.G.,
RA   Smith W.W., Ludwig M.L.;
RT   "The structure of the oxidized form of clostridial flavodoxin at 1.9-A
RT   resolution.";
RL   J. Biol. Chem. 249:4383-4392(1974).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=9063874; DOI=10.1021/bi962180o;
RA   Ludwig M.L., Pattridge K.A., Metzger A.L., Dixon M.M., Eren M., Feng Y.,
RA   Swenson R.P.;
RT   "Control of oxidation-reduction potentials in flavodoxin from Clostridium
RT   beijerinckii: the role of conformation changes.";
RL   Biochemistry 36:1259-1280(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   PDB; 1FLA; X-ray; 1.90 A; A=1-138.
DR   PDB; 1FLD; X-ray; 1.80 A; A=1-138.
DR   PDB; 1FLN; X-ray; 1.90 A; A=1-138.
DR   PDB; 1FVX; X-ray; 1.90 A; A=1-138.
DR   PDB; 2FAX; X-ray; 1.80 A; A=1-136.
DR   PDB; 2FDX; X-ray; 1.65 A; A=1-136.
DR   PDB; 2FLV; X-ray; 1.80 A; A=1-138.
DR   PDB; 2FOX; X-ray; 1.80 A; A=1-138.
DR   PDB; 2FVX; X-ray; 1.80 A; A=1-138.
DR   PDB; 3NLL; X-ray; 2.40 A; A=1-138.
DR   PDB; 4NLL; X-ray; 1.90 A; A=1-138.
DR   PDB; 4NUL; X-ray; 1.90 A; A=1-138.
DR   PDB; 5NLL; X-ray; 1.75 A; A=1-138.
DR   PDB; 5NUL; X-ray; 1.60 A; A=1-138.
DR   PDB; 5ULL; X-ray; 1.80 A; A=1-138.
DR   PDB; 6NUL; X-ray; 1.80 A; A=1-136.
DR   PDBsum; 1FLA; -.
DR   PDBsum; 1FLD; -.
DR   PDBsum; 1FLN; -.
DR   PDBsum; 1FVX; -.
DR   PDBsum; 2FAX; -.
DR   PDBsum; 2FDX; -.
DR   PDBsum; 2FLV; -.
DR   PDBsum; 2FOX; -.
DR   PDBsum; 2FVX; -.
DR   PDBsum; 3NLL; -.
DR   PDBsum; 4NLL; -.
DR   PDBsum; 4NUL; -.
DR   PDBsum; 5NLL; -.
DR   PDBsum; 5NUL; -.
DR   PDBsum; 5ULL; -.
DR   PDBsum; 6NUL; -.
DR   AlphaFoldDB; P00322; -.
DR   SMR; P00322; -.
DR   STRING; 1520.LF65_03122; -.
DR   DrugBank; DB03247; Flavin mononucleotide.
DR   EvolutionaryTrace; P00322; -.
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; IPR010087; Flav_short.
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   TIGRFAMs; TIGR01753; flav_short; 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; Transport.
FT   CHAIN           1..138
FT                   /note="Flavodoxin"
FT                   /id="PRO_0000171613"
FT   DOMAIN          1..136
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           11..25
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           66..73
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   STRAND          81..91
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           94..105
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   STRAND          115..120
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:5NUL"
FT   HELIX           125..136
FT                   /evidence="ECO:0007829|PDB:5NUL"
SQ   SEQUENCE   138 AA;  15332 MW;  98BE3746EC000FF1 CRC64;
     MKIVYWSGTG NTEKMAELIA KGIIESGKDV NTINVSDVNI DELLNEDILI LGCSAMGDEV
     LEESEFEPFI EEISTKISGK KVALFGSYGW GDGKWMRDFE ERMNGYGCVV VETPLIVQNE
     PDEAEQDCIE FGKKIANI