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Protein

NADPH-dependent FMN reductase ArsH

Gene

arsH

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has NADPH-dependent FMN reductase activity and very low azoreductase activity. No activity with NADH.1 Publication

Cofactori

FMN1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi43 – 50FMNBy similarity8

GO - Molecular functioni

  • azobenzene reductase activity Source: UniProtKB
  • FMN binding Source: UniProtKB
  • FMN reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NADP, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH-dependent FMN reductase ArsHCurated (EC:1.-.-.-1 Publication)
Alternative name(s):
Arsenical resistance operon protein ArsHCuratedImported
Gene namesi
Name:arsH1 PublicationImported
Ordered Locus Names:S2709Imported
ORF Names:SF2457T_0606Imported
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004322211 – 255NADPH-dependent FMN reductase ArsHAdd BLAST255

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni17 – 19Combined sources3
Turni24 – 28Combined sources5
Beta strandi36 – 42Combined sources7
Beta strandi45 – 47Combined sources3
Helixi49 – 63Combined sources15
Beta strandi67 – 71Combined sources5
Turni79 – 81Combined sources3
Helixi83 – 85Combined sources3
Helixi88 – 99Combined sources12
Beta strandi101 – 110Combined sources10
Helixi116 – 124Combined sources9
Beta strandi139 – 145Combined sources7
Beta strandi147 – 149Combined sources3
Helixi153 – 164Combined sources12
Beta strandi174 – 176Combined sources3
Helixi179 – 181Combined sources3
Helixi193 – 212Combined sources20
Helixi213 – 215Combined sources3
Helixi216 – 219Combined sources4
Helixi223 – 229Combined sources7
Helixi235 – 238Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FZVX-ray1.70A/B/C/D1-255[»]
ProteinModelPortaliQ7UC03.
SMRiQ7UC03.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7UC03.

Family & Domainsi

Sequence similaritiesi

Belongs to the ArsH family.Curated

Phylogenomic databases

HOGENOMiHOG000112414.
KOiK11811.
OMAiNLSEAHA.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR014063. Arsenate-R_ArsH.
IPR029039. Flavoprotein-like_dom.
IPR005025. FMN_Rdtase-like.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR02690. resist_ArsH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7UC03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLRHLSDPD SLPALDKSFA IERPALGLAP DAPPVRILLL YGSLRARSFS
60 70 80 90 100
RLAVEEAARL LQFFGAETRI FDPSDLPLPD QVQSDDHPAV KELRALSEWS
110 120 130 140 150
EGQVWCSPER HGQITSVMKA QIDHLPLEMA GIRPTQGRTL AVMQVSGGSQ
160 170 180 190 200
SFNAVNTLRL LGRWMRMFTI PNQSSIAKAF QEFDAAGRMK PSPYYDRIAD
210 220 230 240 250
VMEELVRFTA LVRPHREALT DRYSERKAAG HVIDEATDLS SIAIAPQPLP

ESETS
Length:255
Mass (Da):28,400
Last modified:October 1, 2003 - v1
Checksum:i80740B0559A33296
GO

Sequence cautioni

The sequence EFS15380 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014073 Genomic DNA. Translation: AAP17869.1.
ADUV01000006 Genomic DNA. Translation: EFS15380.1. Different initiation.

Genome annotation databases

EnsemblBacteriaiAAP17869; AAP17869; S2709.
EFS15380; EFS15380; SF2457T_0606.
KEGGisfx:S2709.
PATRICi18707056. VBIShiFle31049_2996.
51929987. VBIShiFle203745_0575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014073 Genomic DNA. Translation: AAP17869.1.
ADUV01000006 Genomic DNA. Translation: EFS15380.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FZVX-ray1.70A/B/C/D1-255[»]
ProteinModelPortaliQ7UC03.
SMRiQ7UC03.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP17869; AAP17869; S2709.
EFS15380; EFS15380; SF2457T_0606.
KEGGisfx:S2709.
PATRICi18707056. VBIShiFle31049_2996.
51929987. VBIShiFle203745_0575.

Phylogenomic databases

HOGENOMiHOG000112414.
KOiK11811.
OMAiNLSEAHA.

Miscellaneous databases

EvolutionaryTraceiQ7UC03.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR014063. Arsenate-R_ArsH.
IPR029039. Flavoprotein-like_dom.
IPR005025. FMN_Rdtase-like.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR02690. resist_ArsH. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARREH_SHIFL
AccessioniPrimary (citable) accession number: Q7UC03
Secondary accession number(s): E3XY12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 4, 2015
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete 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.