FLAV_DESVH
ID FLAV_DESVH Reviewed; 148 AA.
AC P00323;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Flavodoxin;
GN OrderedLocusNames=DVU_2680;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3170590; DOI=10.1016/s0021-9258(19)37607-0;
RA Krey G.D., Vanin E.F., Swenson R.P.;
RT "Cloning, nucleotide sequence, and expression of the flavodoxin gene from
RT Desulfovibrio vulgaris (Hildenborough).";
RL J. Biol. Chem. 263:15436-15443(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Curley G.P., Voordouw G.;
RT "Cloning and sequencing of the gene encoding flavodoxin from Desulfovibrio
RT vulgaris Hildenborough.";
RL FEMS Microbiol. Lett. 49:295-299(1988).
RN [3]
RP PROTEIN SEQUENCE.
RX PubMed=402366; DOI=10.1016/s0021-9258(17)40678-8;
RA Dubourdieu M., Fox J.L.;
RT "Amino acid sequence of Desulfovibrio vulgaris flavodoxin.";
RL J. Biol. Chem. 252:1453-1463(1977).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2002503; DOI=10.1016/0022-2836(91)90884-9;
RA Warr W., Tulinsky A., Swenson R.P., Watenpaugh K.D.;
RT "Comparison of the crystal structures of a flavodoxin in its three
RT oxidation states at cryogenic temperatures.";
RL J. Mol. Biol. 218:195-208(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=4521211; DOI=10.1073/pnas.70.12.3857;
RA Watenpaugh K.D., Sieker L.C., Jensen L.H.;
RT "The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at
RT 2.0-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 70:3857-3860(1973).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=4508313; DOI=10.1073/pnas.69.11.3185;
RA Watenpaugh K.D., Sieker L.C., Jensen L.H., Legall J., Dubourdieu M.;
RT "Structure of the oxidized form of a flavodoxin at 2.5-A resolution:
RT resolution of the phase ambiguity by anomalous scattering.";
RL Proc. Natl. Acad. Sci. U.S.A. 69:3185-3188(1972).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9874201; DOI=10.1046/j.1432-1327.1998.2580362.x;
RA Walsh M.A., McCarthy A., O'Farrell P.A., McArdle P., Cunningham P.D.,
RA Mayhew S.G., Higgins T.M.;
RT "X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough)
RT apoflavodoxin-riboflavin complex.";
RL Eur. J. Biochem. 258:362-371(1998).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=8477691; DOI=10.1111/j.1432-1033.1993.tb17746.x;
RA Knauf M.A., Loehr F., Curley G.P., O'Farrell P., Mayhew S.G., Mueller F.,
RA Rueterjans H.;
RT "Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio
RT vulgaris flavodoxin. Sequential assignments and identification of secondary
RT structure elements.";
RL Eur. J. Biochem. 213:167-184(1993).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=8681954; DOI=10.1111/j.1432-1033.1996.0423z.x;
RA Knauf M.A., Loehr F., Bluemel M., Mayhew S.G., Rueterjans H.;
RT "NMR investigation of the solution conformation of oxidized flavodoxin from
RT Desulfovibrio vulgaris. Determination of the tertiary structure and
RT detection of protein-bound water molecules.";
RL Eur. J. Biochem. 238:423-434(1996).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=8477184; DOI=10.1007/bf00178258;
RA Stockman B.J., Euvrard A., Kloosterman D.A., Scahill T.A., Swenson R.P.;
RT "1H and 15N resonance assignments and solution secondary structure of
RT oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear
RT three-dimensional NMR spectroscopy.";
RL J. Biomol. NMR 3:133-149(1993).
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 EMBL; J04033; AAA23367.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS97152.1; -; Genomic_DNA.
DR PIR; A31991; FXDV.
DR RefSeq; WP_010939949.1; NC_002937.3.
DR RefSeq; YP_011892.1; NC_002937.3.
DR PDB; 1AKQ; X-ray; 1.90 A; A=2-148.
DR PDB; 1AKR; X-ray; 1.58 A; A=2-148.
DR PDB; 1AKT; X-ray; 1.80 A; A=2-148.
DR PDB; 1AKU; X-ray; 1.90 A; A=2-148.
DR PDB; 1AKV; X-ray; 2.00 A; A=2-148.
DR PDB; 1AKW; X-ray; 1.75 A; A=2-148.
DR PDB; 1AZL; X-ray; 1.80 A; A=2-148.
DR PDB; 1BU5; X-ray; 1.83 A; A/B=2-148.
DR PDB; 1C7E; X-ray; 2.25 A; A/B=2-148.
DR PDB; 1C7F; X-ray; 2.00 A; A/B=2-148.
DR PDB; 1F4P; X-ray; 1.30 A; A=2-148.
DR PDB; 1FX1; X-ray; 2.00 A; A=1-148.
DR PDB; 1I1O; X-ray; 2.00 A; A=3-148.
DR PDB; 1J8Q; X-ray; 1.35 A; A=2-148.
DR PDB; 1J9E; X-ray; 1.44 A; A=2-148.
DR PDB; 1J9G; X-ray; 2.40 A; A=2-148.
DR PDB; 1WSB; X-ray; 1.80 A; A=1-148.
DR PDB; 1WSW; X-ray; 1.69 A; A=1-148.
DR PDB; 1XT6; X-ray; 1.80 A; A=3-148.
DR PDB; 1XYV; X-ray; 1.79 A; A=1-148.
DR PDB; 1XYY; X-ray; 1.70 A; A=1-148.
DR PDB; 2FX2; X-ray; 1.90 A; A=3-148.
DR PDB; 3FX2; X-ray; 1.90 A; A=3-148.
DR PDB; 4FX2; X-ray; 1.90 A; A=3-148.
DR PDB; 5FX2; X-ray; 1.90 A; A=3-148.
DR PDB; 5TGZ; X-ray; 2.80 A; A=2-148.
DR PDB; 5V56; X-ray; 2.90 A; A/B=6-148.
DR PDB; 5V57; X-ray; 3.00 A; A/B=6-148.
DR PDB; 5XR8; X-ray; 2.95 A; A=3-148.
DR PDB; 5XRA; X-ray; 2.80 A; A=3-148.
DR PDB; 5YOB; X-ray; 1.14 A; A=3-148.
DR PDB; 5YOC; X-ray; 1.50 A; A=3-148.
DR PDB; 5YOE; X-ray; 1.35 A; A=3-148.
DR PDB; 5YOG; X-ray; 1.42 A; A=3-148.
DR PDB; 5ZKP; X-ray; 2.81 A; A=3-148.
DR PDB; 6LI0; X-ray; 2.20 A; A=3-148.
DR PDB; 6LI1; X-ray; 2.90 A; A=3-148.
DR PDB; 7DDZ; X-ray; 2.80 A; A=3-148.
DR PDB; 7EPE; X-ray; 2.50 A; A=3-148.
DR PDB; 7EPF; X-ray; 2.70 A; A=3-148.
DR PDB; 7K15; X-ray; 2.88 A; A=2-148.
DR PDB; 7V3Z; X-ray; 3.29 A; A=3-148.
DR PDBsum; 1AKQ; -.
DR PDBsum; 1AKR; -.
DR PDBsum; 1AKT; -.
DR PDBsum; 1AKU; -.
DR PDBsum; 1AKV; -.
DR PDBsum; 1AKW; -.
DR PDBsum; 1AZL; -.
DR PDBsum; 1BU5; -.
DR PDBsum; 1C7E; -.
DR PDBsum; 1C7F; -.
DR PDBsum; 1F4P; -.
DR PDBsum; 1FX1; -.
DR PDBsum; 1I1O; -.
DR PDBsum; 1J8Q; -.
DR PDBsum; 1J9E; -.
DR PDBsum; 1J9G; -.
DR PDBsum; 1WSB; -.
DR PDBsum; 1WSW; -.
DR PDBsum; 1XT6; -.
DR PDBsum; 1XYV; -.
DR PDBsum; 1XYY; -.
DR PDBsum; 2FX2; -.
DR PDBsum; 3FX2; -.
DR PDBsum; 4FX2; -.
DR PDBsum; 5FX2; -.
DR PDBsum; 5TGZ; -.
DR PDBsum; 5V56; -.
DR PDBsum; 5V57; -.
DR PDBsum; 5XR8; -.
DR PDBsum; 5XRA; -.
DR PDBsum; 5YOB; -.
DR PDBsum; 5YOC; -.
DR PDBsum; 5YOE; -.
DR PDBsum; 5YOG; -.
DR PDBsum; 5ZKP; -.
DR PDBsum; 6LI0; -.
DR PDBsum; 6LI1; -.
DR PDBsum; 7DDZ; -.
DR PDBsum; 7EPE; -.
DR PDBsum; 7EPF; -.
DR PDBsum; 7K15; -.
DR PDBsum; 7V3Z; -.
DR AlphaFoldDB; P00323; -.
DR BMRB; P00323; -.
DR SMR; P00323; -.
DR STRING; 882.DVU_2680; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR PaxDb; P00323; -.
DR EnsemblBacteria; AAS97152; AAS97152; DVU_2680.
DR KEGG; dvu:DVU_2680; -.
DR PATRIC; fig|882.5.peg.2425; -.
DR eggNOG; COG0716; Bacteria.
DR HOGENOM; CLU_051402_4_2_7; -.
DR OMA; ENCRAYG; -.
DR PhylomeDB; P00323; -.
DR EvolutionaryTrace; P00323; -.
DR Proteomes; UP000002194; Chromosome.
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 Pfam; PF00258; Flavodoxin_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
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; Reference proteome; Transport.
FT CHAIN 1..148
FT /note="Flavodoxin"
FT /id="PRO_0000171620"
FT DOMAIN 4..145
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT CONFLICT 28
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5YOB"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5YOB"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:5YOB"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:5YOB"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5YOB"
FT TURN 44..49
FT /evidence="ECO:0007829|PDB:5YOB"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5YOB"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5YOB"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5YOB"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:5YOB"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5YOB"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5YOB"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5YOB"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:5YOB"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5YOB"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:5YOB"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:5YOB"
SQ SEQUENCE 148 AA; 15823 MW; E07630E7047ABD3F CRC64;
MPKALIVYGS TTGNTEYTAE TIARELADAG YEVDSRDAAS VEAGGLFEGF DLVLLGCSTW
GDDSIELQDD FIPLFDSLEE TGAQGRKVAC FGCGDSSYEY FCGAVDAIEE KLKNLGAEIV
QDGLRIDGDP RAARDDIVGW AHDVRGAI
