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Protein

Flavodoxin

Gene

DVU_2680

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Low-potential electron donor to a number of redox enzymes.

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciDVUL882:GJIL-2748-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavodoxin
Gene namesi
Ordered Locus Names:DVU_2680
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 148148FlavodoxinPRO_0000171620Add
BLAST

Proteomic databases

PaxDbiP00323.

Interactioni

Protein-protein interaction databases

STRINGi882.DVU2680.

Structurei

Secondary structure

1
148
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi11 – 133Combined sources
Helixi14 – 2916Combined sources
Beta strandi32 – 376Combined sources
Helixi38 – 403Combined sources
Turni44 – 496Combined sources
Beta strandi51 – 577Combined sources
Beta strandi62 – 643Combined sources
Turni69 – 713Combined sources
Helixi72 – 765Combined sources
Helixi78 – 803Combined sources
Beta strandi87 – 948Combined sources
Beta strandi98 – 1003Combined sources
Helixi103 – 11412Combined sources
Beta strandi124 – 1285Combined sources
Helixi130 – 1334Combined sources
Helixi134 – 14512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKQX-ray1.90A2-148[»]
1AKRX-ray1.58A2-148[»]
1AKTX-ray1.80A2-148[»]
1AKUX-ray1.90A2-148[»]
1AKVX-ray2.00A2-148[»]
1AKWX-ray1.75A2-148[»]
1AZLX-ray1.80A2-148[»]
1BU5X-ray1.83A/B2-148[»]
1C7EX-ray2.25A/B2-148[»]
1C7FX-ray2.00A/B2-148[»]
1F4PX-ray1.30A2-148[»]
1FX1X-ray2.00A1-148[»]
1I1OX-ray2.00A3-148[»]
1J8QX-ray1.35A2-148[»]
1J9EX-ray1.44A2-148[»]
1J9GX-ray2.40A2-148[»]
1WSBX-ray1.80A1-148[»]
1WSWX-ray1.69A1-148[»]
1XT6X-ray1.80A3-148[»]
1XYVX-ray1.79A1-148[»]
1XYYX-ray1.70A1-148[»]
2FX2X-ray1.90A3-148[»]
3FX2X-ray1.90A3-148[»]
4FX2X-ray1.90A3-148[»]
5FX2X-ray1.90A3-148[»]
ProteinModelPortaliP00323.
SMRiP00323. Positions 2-148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 145142Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the flavodoxin family.Curated
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG41082EJ. Bacteria.
COG0716. LUCA.
OMAiTACFGSG.
OrthoDBiEOG6RG039.
PhylomeDBiP00323.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR010087. Flav_short.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001226. Flavodoxin_CS.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
[Graphical view]
PRINTSiPR00369. FLAVODOXIN.
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR01753. flav_short. 1 hit.
PROSITEiPS00201. FLAVODOXIN. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKALIVYGS TTGNTEYTAE TIARELADAG YEVDSRDAAS VEAGGLFEGF
60 70 80 90 100
DLVLLGCSTW GDDSIELQDD FIPLFDSLEE TGAQGRKVAC FGCGDSSYEY
110 120 130 140
FCGAVDAIEE KLKNLGAEIV QDGLRIDGDP RAARDDIVGW AHDVRGAI
Length:148
Mass (Da):15,823
Last modified:November 1, 1990 - v2
Checksum:iE07630E7047ABD3F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281D → N (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04033 Genomic DNA. Translation: AAA23367.1.
AE017285 Genomic DNA. Translation: AAS97152.1.
PIRiA31991. FXDV.
RefSeqiWP_010939949.1. NC_002937.3.
YP_011892.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS97152; AAS97152; DVU_2680.
GeneIDi2795051.
KEGGidvu:DVU2680.
PATRICi32064950. VBIDesVul119526_2425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04033 Genomic DNA. Translation: AAA23367.1.
AE017285 Genomic DNA. Translation: AAS97152.1.
PIRiA31991. FXDV.
RefSeqiWP_010939949.1. NC_002937.3.
YP_011892.1. NC_002937.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKQX-ray1.90A2-148[»]
1AKRX-ray1.58A2-148[»]
1AKTX-ray1.80A2-148[»]
1AKUX-ray1.90A2-148[»]
1AKVX-ray2.00A2-148[»]
1AKWX-ray1.75A2-148[»]
1AZLX-ray1.80A2-148[»]
1BU5X-ray1.83A/B2-148[»]
1C7EX-ray2.25A/B2-148[»]
1C7FX-ray2.00A/B2-148[»]
1F4PX-ray1.30A2-148[»]
1FX1X-ray2.00A1-148[»]
1I1OX-ray2.00A3-148[»]
1J8QX-ray1.35A2-148[»]
1J9EX-ray1.44A2-148[»]
1J9GX-ray2.40A2-148[»]
1WSBX-ray1.80A1-148[»]
1WSWX-ray1.69A1-148[»]
1XT6X-ray1.80A3-148[»]
1XYVX-ray1.79A1-148[»]
1XYYX-ray1.70A1-148[»]
2FX2X-ray1.90A3-148[»]
3FX2X-ray1.90A3-148[»]
4FX2X-ray1.90A3-148[»]
5FX2X-ray1.90A3-148[»]
ProteinModelPortaliP00323.
SMRiP00323. Positions 2-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi882.DVU2680.

Proteomic databases

PaxDbiP00323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS97152; AAS97152; DVU_2680.
GeneIDi2795051.
KEGGidvu:DVU2680.
PATRICi32064950. VBIDesVul119526_2425.

Phylogenomic databases

eggNOGiENOG41082EJ. Bacteria.
COG0716. LUCA.
OMAiTACFGSG.
OrthoDBiEOG6RG039.
PhylomeDBiP00323.

Enzyme and pathway databases

BioCyciDVUL882:GJIL-2748-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00323.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR010087. Flav_short.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001226. Flavodoxin_CS.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
[Graphical view]
PRINTSiPR00369. FLAVODOXIN.
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR01753. flav_short. 1 hit.
PROSITEiPS00201. FLAVODOXIN. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, nucleotide sequence, and expression of the flavodoxin gene from Desulfovibrio vulgaris (Hildenborough)."
    Krey G.D., Vanin E.F., Swenson R.P.
    J. Biol. Chem. 263:15436-15443(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and sequencing of the gene encoding flavodoxin from Desulfovibrio vulgaris Hildenborough."
    Curley G.P., Voordouw G.
    FEMS Microbiol. Lett. 49:295-299(1988)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Amino acid sequence of Desulfovibrio vulgaris flavodoxin."
    Dubourdieu M., Fox J.L.
    J. Biol. Chem. 252:1453-1463(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
  5. "Comparison of the crystal structures of a flavodoxin in its three oxidation states at cryogenic temperatures."
    Warr W., Tulinsky A., Swenson R.P., Watenpaugh K.D.
    J. Mol. Biol. 218:195-208(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  6. "The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at 2.0-A resolution."
    Watenpaugh K.D., Sieker L.C., Jensen L.H.
    Proc. Natl. Acad. Sci. U.S.A. 70:3857-3860(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  7. "Structure of the oxidized form of a flavodoxin at 2.5-A resolution: resolution of the phase ambiguity by anomalous scattering."
    Watenpaugh K.D., Sieker L.C., Jensen L.H., Legall J., Dubourdieu M.
    Proc. Natl. Acad. Sci. U.S.A. 69:3185-3188(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  8. "X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough) apoflavodoxin-riboflavin complex."
    Walsh M.A., McCarthy A., O'Farrell P.A., McArdle P., Cunningham P.D., Mayhew S.G., Higgins T.M.
    Eur. J. Biochem. 258:362-371(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  9. "Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio vulgaris flavodoxin. Sequential assignments and identification of secondary structure elements."
    Knauf M.A., Loehr F., Curley G.P., O'Farrell P., Mayhew S.G., Mueller F., Rueterjans H.
    Eur. J. Biochem. 213:167-184(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary structure and detection of protein-bound water molecules."
    Knauf M.A., Loehr F., Bluemel M., Mayhew S.G., Rueterjans H.
    Eur. J. Biochem. 238:423-434(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  11. "1H and 15N resonance assignments and solution secondary structure of oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear three-dimensional NMR spectroscopy."
    Stockman B.J., Euvrard A., Kloosterman D.A., Scahill T.A., Swenson R.P.
    J. Biomol. NMR 3:133-149(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiFLAV_DESVH
AccessioniPrimary (citable) accession number: P00323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: January 20, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.