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Protein

Flavodoxin

Gene

isiB

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed-Annotation score: Annotation score: 3 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, Stress response, Transport

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1541-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavodoxin
Gene namesi
Name:isiB
Ordered Locus Names:Synpcc7942_1541
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
Proteomesi
  • UP000002717 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 170169FlavodoxinPRO_0000171644Add
BLAST

Expressioni

Inductioni

By iron stress.

Interactioni

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1541.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi11 – 133Combined sources
Helixi14 – 2613Combined sources
Turni29 – 313Combined sources
Beta strandi32 – 365Combined sources
Helixi37 – 393Combined sources
Helixi42 – 476Combined sources
Beta strandi49 – 546Combined sources
Turni59 – 613Combined sources
Helixi65 – 706Combined sources
Helixi71 – 766Combined sources
Beta strandi83 – 897Combined sources
Turni92 – 976Combined sources
Helixi101 – 11212Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi138 – 1447Combined sources
Turni146 – 1483Combined sources
Helixi150 – 1523Combined sources
Helixi153 – 16715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZHX-ray1.86A2-170[»]
1CZKX-ray1.90A2-170[»]
1CZLX-ray1.80A2-170[»]
1CZNX-ray1.70A2-170[»]
1CZOX-ray1.85A2-170[»]
1CZRX-ray1.90A2-170[»]
1CZUX-ray2.00A2-170[»]
1D03X-ray1.85A2-170[»]
1D04X-ray1.85A2-170[»]
1OFVX-ray1.70A2-170[»]
ProteinModelPortaliP10340.
SMRiP10340. Positions 2-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10340.

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.
KOiK03839.
OrthoDBiEOG6C5RTW.

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.

P10340-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIGLFYGT QTGVTQTIAE SIQQEFGGES IVDLNDIANA DASDLNAYDY
60 70 80 90 100
LIIGCPTWNV GELQSDWEGI YDDLDSVNFQ GKKVAYFGAG DQVGYSDNFQ
110 120 130 140 150
DAMGILEEKI SSLGSQTVGY WPIEGYDFNE SKAVRNNQFV GLAIDEDNQP
160 170
DLTKNRIKTW VSQLKSEFGL
Length:170
Mass (Da):18,778
Last modified:January 23, 2007 - v3
Checksum:i7291AEF23DCA0345
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551C → S AA sequence (PubMed:6406674).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19116 Genomic DNA. Translation: AAA22050.1.
CP000100 Genomic DNA. Translation: ABB57571.1.
RefSeqiWP_011242314.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB57571; ABB57571; Synpcc7942_1541.
KEGGisyf:Synpcc7942_1541.
PATRICi23788451. VBISynElo51371_1750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19116 Genomic DNA. Translation: AAA22050.1.
CP000100 Genomic DNA. Translation: ABB57571.1.
RefSeqiWP_011242314.1. NC_007604.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZHX-ray1.86A2-170[»]
1CZKX-ray1.90A2-170[»]
1CZLX-ray1.80A2-170[»]
1CZNX-ray1.70A2-170[»]
1CZOX-ray1.85A2-170[»]
1CZRX-ray1.90A2-170[»]
1CZUX-ray2.00A2-170[»]
1D03X-ray1.85A2-170[»]
1D04X-ray1.85A2-170[»]
1OFVX-ray1.70A2-170[»]
ProteinModelPortaliP10340.
SMRiP10340. Positions 2-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1541.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB57571; ABB57571; Synpcc7942_1541.
KEGGisyf:Synpcc7942_1541.
PATRICi23788451. VBISynElo51371_1750.

Phylogenomic databases

eggNOGiENOG4105MHQ. Bacteria.
COG0716. LUCA.
HOGENOMiHOG000030543.
KOiK03839.
OrthoDBiEOG6C5RTW.

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1541-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP10340.

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, sequence analysis, and transcriptional studies of the flavodoxin gene from Anacystis nidulans R2."
    Laudenbach D.E., Reith M.E., Straus N.A.
    J. Bacteriol. 170:258-265(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.
  3. Cited for: PROTEIN SEQUENCE OF 2-56, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  4. "Refined structures of oxidized flavodoxin from Anacystis nidulans."
    Drennan C.L., Pattridge K.A., Weber C.H., Metzger A.L., Hoover D.M., Ludwig M.L.
    J. Mol. Biol. 294:711-724(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  5. "Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans. Structural determinants of the redox potentials."
    Hoover D.M., Drennan C.L., Metzger A.L., Osborne C., Weber C.H., Pattridge K.A., Ludwig M.L.
    J. Mol. Biol. 294:725-743(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
  6. "1H and 15N resonance assignments of oxidized flavodoxin from Anacystis nidulans with 3D NMR."
    Clubb R.T., Thanabal V., Osborne C., Wagner G.
    Biochemistry 30:7718-7730(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiFLAV_SYNE7
AccessioniPrimary (citable) accession number: P10340
Secondary accession number(s): Q31MZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 121 of the entry and version 3 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.