ID   FLAV_MEGG1              Reviewed;         146 AA.
AC   Q01095;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Flavodoxin;
OS   Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS   B-1759) (Desulfovibrio gigas).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Megalodesulfovibrio.
OX   NCBI_TaxID=1121448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RX   PubMed=1627649; DOI=10.1016/0167-4781(92)90034-w;
RA   Helms L.R., Swenson R.P.;
RT   "The primary structures of the flavodoxins from two strains of
RT   Desulfovibrio gigas. Cloning and nucleotide sequence of the structural
RT   genes.";
RL   Biochim. Biophys. Acta 1131:325-328(1992).
CC   -!- FUNCTION: Electron-transfer proteins that function in various electron
CC       transport systems in microorganisms. Functionally interchangeable with
CC       ferredoxin.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   EMBL; X64766; CAA46013.1; -; Genomic_DNA.
DR   PIR; S24311; S24311.
DR   RefSeq; WP_021760293.1; NZ_AUBO01000056.1.
DR   PDB; 4HEQ; X-ray; 1.30 A; A/B=1-146.
DR   PDBsum; 4HEQ; -.
DR   AlphaFoldDB; Q01095; -.
DR   SMR; Q01095; -.
DR   STRING; 1121448.DGI_1615; -.
DR   OrthoDB; 9790745at2; -.
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; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   NCBIfam; TIGR01753; flav_short; 1.
DR   PANTHER; PTHR42809:SF1; FLAVODOXIN 1; 1.
DR   PANTHER; PTHR42809; FLAVODOXIN 2; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   SUPFAM; SSF52218; Flavoproteins; 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; Transport.
FT   CHAIN           1..146
FT                   /note="Flavodoxin"
FT                   /id="PRO_0000171617"
FT   DOMAIN          4..143
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   HELIX           14..28
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   TURN            44..49
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   HELIX           71..76
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   STRAND          87..94
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   STRAND          124..129
FT                   /evidence="ECO:0007829|PDB:4HEQ"
FT   HELIX           132..145
FT                   /evidence="ECO:0007829|PDB:4HEQ"
SQ   SEQUENCE   146 AA;  15470 MW;  95D9E73B1FCF1403 CRC64;
     MPKALIVYGS TTGNTEGVAE AIAKTLNSEG METTVVNVAD VTAPGLAEGY DVVLLGCSTW
     GDDEIELQED FVPLYEDLDR AGLKDKKVGV FGCGDSSYTY FCGAVDVIEK KAEELGATLV
     ASSLKIDGEP DSAEVLDWAR EVLARV
//