ID   FLAV_CHOCR              Reviewed;         173 AA.
AC   P14070;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Flavodoxin;
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2597140; DOI=10.1042/bj2630981;
RA   Wakabayashi S., Kimura K., Matsubara H., Rogers L.J.;
RT   "The amino acid sequence of a flavodoxin from the eukaryotic red alga
RT   Chondrus crispus.";
RL   Biochem. J. 263:981-984(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-34.
RA   Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;
RT   "N-terminal amino acid sequences of flavodoxins from Chondrus crispus and
RT   Nostoc strain MAC.";
RL   Phytochemistry 25:2113-2115(1986).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX   PubMed=2394748; DOI=10.1016/s0021-9258(18)55469-7;
RA   Fukuyama K., Wakabayashi S., Matsubara H., Rogers L.J.;
RT   "Tertiary structure of oxidized flavodoxin from an eukaryotic red alga
RT   Chondrus crispus at 2.35-A resolution. Localization of charged residues and
RT   implication for interaction with electron transfer partners.";
RL   J. Biol. Chem. 265:15804-15812(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=1602481; DOI=10.1016/0022-2836(92)90400-e;
RA   Fukuyama K., Matsubara H., Rogers L.J.;
RT   "Crystal structure of oxidized flavodoxin from a red alga Chondrus crispus
RT   refined at 1.8-A resolution. Description of the flavin mononucleotide
RT   binding site.";
RL   J. Mol. Biol. 225:775-789(1992).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; S06648; S06648.
DR   PDB; 2FCR; X-ray; 1.80 A; A=1-173.
DR   PDBsum; 2FCR; -.
DR   AlphaFoldDB; P14070; -.
DR   SMR; P14070; -.
DR   EnsemblPlants; CDF32621; CDF32621; CHC_T00009139001.
DR   Gramene; CDF32621; CDF32621; CHC_T00009139001.
DR   OMA; ILGISTW; -.
DR   EvolutionaryTrace; P14070; -.
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; Transport.
FT   CHAIN           1..173
FT                   /note="Flavodoxin"
FT                   /id="PRO_0000171612"
FT   DOMAIN          2..168
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   CONFLICT        29
FT                   /note="D -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="D -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           12..24
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           69..75
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           105..115
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:2FCR"
FT   HELIX           156..171
FT                   /evidence="ECO:0007829|PDB:2FCR"
SQ   SEQUENCE   173 AA;  18871 MW;  EF1F3A3554CA4166 CRC64;
     KIGIFFSTST GNTTEVADFI GKTLGAKADA PIDVDDVTDP QALKDYDLLF LGAPTWNTGA
     DTERSGTSWD EFLYDKLPEV DMKDLPVAIF GLGDAEGYPD NFCDAIEEIH DCFAKQGAKP
     VGFSNPDDYD YEESKSVRDG KFLGLPLDMV NDQIPMEKRV AGWVEAVVSE TGV