ID   FLAW_DESDA              Reviewed;         148 AA.
AC   P80312; B8J2S8;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Flavodoxin;
GN   OrderedLocusNames=Ddes_1951;
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 / DSM 6949 / MB;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-146.
RX   PubMed=8143752; DOI=10.1111/j.1432-1033.1994.tb18703.x;
RA   Caldeira J., Palma P.N., Regalla M., Lampreia J., Calvete J.J.,
RA   Schaefer W., Legall J., Moura I., Moura J.J.G.;
RT   "Primary sequence, oxidation-reduction potentials and tertiary-structure
RT   prediction of Desulfovibrio desulfuricans ATCC 27774 flavodoxin.";
RL   Eur. J. Biochem. 220:987-995(1994).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) are -410 mV and -100 mV.;
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   EMBL; CP001358; ACL49847.1; -; Genomic_DNA.
DR   PIR; S42570; S42570.
DR   RefSeq; WP_012625571.1; NC_011883.1.
DR   PDB; 3KAP; X-ray; 2.05 A; A=2-148.
DR   PDB; 3KAQ; X-ray; 2.25 A; A=2-148.
DR   PDBsum; 3KAP; -.
DR   PDBsum; 3KAQ; -.
DR   AlphaFoldDB; P80312; -.
DR   SMR; P80312; -.
DR   STRING; 525146.Ddes_1951; -.
DR   EnsemblBacteria; ACL49847; ACL49847; Ddes_1951.
DR   KEGG; dds:Ddes_1951; -.
DR   eggNOG; COG0716; Bacteria.
DR   HOGENOM; CLU_051402_4_2_7; -.
DR   OMA; ENCRAYG; -.
DR   OrthoDB; 1961680at2; -.
DR   EvolutionaryTrace; P80312; -.
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..148
FT                   /note="Flavodoxin"
FT                   /id="PRO_0000171616"
FT   DOMAIN          4..145
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   CONFLICT        113
FT                   /note="R -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="C -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   HELIX           14..28
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   TURN            44..49
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:3KAQ"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   STRAND          87..94
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   HELIX           104..114
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   STRAND          124..128
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:3KAP"
FT   HELIX           134..147
FT                   /evidence="ECO:0007829|PDB:3KAP"
SQ   SEQUENCE   148 AA;  15566 MW;  8ECA75124F8FACF9 CRC64;
     MSKVLILFGS STGNTESIAQ KLEELVAAGG HEVTLLNAAE ASADNLADGY DAVLMGCSAW
     GMEDLELQDD FAPLFDEMEN MGLKGKKLAA FASGDMEYEH YCGAVPAIEE KARGLGAEVI
     CEGLKIEGDA SSDPDAVSAF AEDVLKKL