ID   FLAV_MEGEL              Reviewed;         137 AA.
AC   P00321;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Flavodoxin;
OS   Megasphaera elsdenii.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=907;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927;
RX   PubMed=4711610; DOI=10.1016/s0021-9258(19)43779-4;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "The primary structure of Peptostreptococcus elsdenii flavodoxin.";
RL   J. Biol. Chem. 248:4354-4366(1973).
RN   [2]
RP   SEQUENCE REVISION TO 78-82.
RX   PubMed=4843143; DOI=10.1016/s0021-9258(19)42431-9;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "Correction of the amino acid sequence of Peptostreptococcus elsdenii
RT   flavodoxin.";
RL   J. Biol. Chem. 249:4397-4397(1974).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-41 AND 136-137.
RC   STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927;
RX   PubMed=5126921; DOI=10.1021/bi00792a009;
RA   Tanaka M., Haniu M., Matsueda G., Yasunobu K.T., Mayhew S., Massey V.;
RT   "Amino- and carboxyl-terminal amino acid sequences of the
RT   Peptostreptococcus eisdenii and Clostridium pasteurianum flavodoxins.";
RL   Biochemistry 10:3041-3046(1971).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=2161759; DOI=10.1111/j.1432-1033.1990.tb15527.x;
RA   van Mierlo C.P.M., Mueller F., Vervoort J.;
RT   "Secondary and tertiary structure characteristics of Megasphaera elsdenii
RT   flavodoxin in the reduced state as determined by two-dimensional 1H NMR.";
RL   Eur. J. Biochem. 189:589-600(1990).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=2253614; DOI=10.1111/j.1432-1033.1990.tb19444.x;
RA   van Mierlo C.P.M., Lijnzaad P., Vervoort J., Mueller F., Berendsen H.J.C.,
RA   de Vlieg J.;
RT   "Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin
RT   and some implications, as determined by two-dimensional 1H-NMR and
RT   restrained molecular dynamics.";
RL   Eur. J. Biochem. 194:185-198(1990).
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   PIR; A92137; FXME.
DR   RefSeq; WP_014015302.1; NZ_JRPS01000009.1.
DR   PDB; 2FZ5; NMR; -; A=1-137.
DR   PDBsum; 2FZ5; -.
DR   AlphaFoldDB; P00321; -.
DR   BMRB; P00321; -.
DR   SMR; P00321; -.
DR   EvolutionaryTrace; P00321; -.
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..137
FT                   /note="Flavodoxin"
FT                   /id="PRO_0000171639"
FT   DOMAIN          2..137
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   HELIX           12..26
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   STRAND          31..35
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   HELIX           41..45
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   STRAND          82..91
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   HELIX           95..106
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   STRAND          110..123
FT                   /evidence="ECO:0007829|PDB:2FZ5"
FT   HELIX           126..135
FT                   /evidence="ECO:0007829|PDB:2FZ5"
SQ   SEQUENCE   137 AA;  14550 MW;  86BD744412D6F869 CRC64;
     MVEIVYWSGT GNTEAMANEI EAAVKAAGAD VESVRFEDTN VDDVASKDVI LLGCPAMGSE
     ELEDSVVEPF FTDLAPKLKG KKVGLFGSYG WGSGEWMDAW KQRTEDTGAT VIGTAIVNEM
     PDNAPECKEL GEAAAKA