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Protein

Flavodoxin-1

Gene

fldA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase.Curated1 Publication

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciEcoCyc:FLAVODOXIN1-MONOMER.
ECOL316407:JW0671-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavodoxin-1
Gene namesi
Name:fldA
Ordered Locus Names:b0684, JW0671
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10318. fldA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 176175Flavodoxin-1PRO_0000171622Add
BLAST

Proteomic databases

EPDiP61949.
PaxDbiP61949.
PRIDEiP61949.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
recXP335963EBI-550021,EBI-1129990
ydaWP760662EBI-550021,EBI-9142914

Protein-protein interaction databases

BioGridi4261909. 10 interactions.
DIPiDIP-48242N.
IntActiP61949. 29 interactions.
MINTiMINT-1239730.
STRINGi511145.b0684.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi11 – 133Combined sources
Helixi14 – 2613Combined sources
Turni28 – 303Combined sources
Beta strandi31 – 355Combined sources
Helixi36 – 383Combined sources
Helixi41 – 455Combined sources
Beta strandi48 – 536Combined sources
Turni58 – 603Combined sources
Helixi64 – 7310Combined sources
Beta strandi82 – 887Combined sources
Turni91 – 966Combined sources
Helixi100 – 10910Combined sources
Turni110 – 1134Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi138 – 1447Combined sources
Turni146 – 1483Combined sources
Turni150 – 1523Combined sources
Helixi153 – 16816Combined sources
Helixi170 – 1734Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG9X-ray1.80A/B2-176[»]
1AHNX-ray2.60A2-176[»]
2MOKNMR-A1-176[»]
ProteinModelPortaliP61949.
SMRiP61949. Positions 2-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61949.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 165162Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105MHQ. Bacteria.
COG0716. LUCA.
HOGENOMiHOG000030543.
InParanoidiP61949.
KOiK03839.
OMAiASKGMAD.
OrthoDBiEOG6C5RTW.
PhylomeDBiP61949.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR001226. Flavodoxin_CS.
IPR010086. Flavodoxin_lc.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
[Graphical view]
PIRSFiPIRSF038996. FldA. 1 hit.
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR01752. flav_long. 1 hit.
PROSITEiPS00201. FLAVODOXIN. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL
60 70 80 90 100
LLGIPTWYYG EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD
110 120 130 140 150
ALGTIRDIIE PRGATIVGHW PTAGYHFEAS KGLADDDHFV GLAIDEDRQP
160 170
ELTAERVEKW VKQISEELHL DEILNA
Length:176
Mass (Da):19,737
Last modified:January 23, 2007 - v2
Checksum:i8878DA1A8EAA55BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59426 Genomic DNA. Translation: AAA23789.1.
U00096 Genomic DNA. Translation: AAC73778.1.
AP009048 Genomic DNA. Translation: BAA35333.1.
PIRiA37319.
RefSeqiNP_415210.1. NC_000913.3.
WP_001018618.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73778; AAC73778; b0684.
BAA35333; BAA35333; BAA35333.
GeneIDi945293.
KEGGiecj:JW0671.
eco:b0684.
PATRICi32116561. VBIEscCol129921_0713.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59426 Genomic DNA. Translation: AAA23789.1.
U00096 Genomic DNA. Translation: AAC73778.1.
AP009048 Genomic DNA. Translation: BAA35333.1.
PIRiA37319.
RefSeqiNP_415210.1. NC_000913.3.
WP_001018618.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG9X-ray1.80A/B2-176[»]
1AHNX-ray2.60A2-176[»]
2MOKNMR-A1-176[»]
ProteinModelPortaliP61949.
SMRiP61949. Positions 2-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261909. 10 interactions.
DIPiDIP-48242N.
IntActiP61949. 29 interactions.
MINTiMINT-1239730.
STRINGi511145.b0684.

Proteomic databases

EPDiP61949.
PaxDbiP61949.
PRIDEiP61949.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73778; AAC73778; b0684.
BAA35333; BAA35333; BAA35333.
GeneIDi945293.
KEGGiecj:JW0671.
eco:b0684.
PATRICi32116561. VBIEscCol129921_0713.

Organism-specific databases

EchoBASEiEB0314.
EcoGeneiEG10318. fldA.

Phylogenomic databases

eggNOGiENOG4105MHQ. Bacteria.
COG0716. LUCA.
HOGENOMiHOG000030543.
InParanoidiP61949.
KOiK03839.
OMAiASKGMAD.
OrthoDBiEOG6C5RTW.
PhylomeDBiP61949.

Enzyme and pathway databases

BioCyciEcoCyc:FLAVODOXIN1-MONOMER.
ECOL316407:JW0671-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP61949.
PROiP61949.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR001226. Flavodoxin_CS.
IPR010086. Flavodoxin_lc.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
[Graphical view]
PIRSFiPIRSF038996. FldA. 1 hit.
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR01752. flav_long. 1 hit.
PROSITEiPS00201. FLAVODOXIN. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, cloning, mapping, and nucleotide sequencing of the gene encoding flavodoxin in Escherichia coli."
    Osborne C., Chen L.-M., Matthews R.G.
    J. Bacteriol. 173:1729-1737(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities."
    Jenkins C.M., Waterman M.R.
    J. Biol. Chem. 269:27401-27408(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  7. "The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of Cob(II)alamin enzyme."
    Jarrett J.T., Hoover D.M., Ludwig M.L., Matthews R.G.
    Biochemistry 37:12649-12658(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN COBALT REDUCTION OF COB(II)ALAMIN.
  8. "NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin."
    Ponstingl H., Otting G.
    Eur. J. Biochem. 244:384-399(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8-A resolution."
    Hoover D.M., Ludwig M.L.
    Protein Sci. 6:2525-2537(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiFLAV_ECOLI
AccessioniPrimary (citable) accession number: P61949
Secondary accession number(s): P23243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 108 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.