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Protein

Monodehydroascorbate reductase, seedling isozyme

Gene
N/A
Organism
Cucumis sativus (Cucumber)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process.

Catalytic activityi

NADH + 2 monodehydroascorbate = NAD+ + 2 ascorbate.By similarity

Cofactori

FADUniRule annotationCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 2418FADBy similarityAdd
BLAST
Nucleotide bindingi165 – 18218NADBy similarityAdd
BLAST
Nucleotide bindingi191 – 1955FADBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Monodehydroascorbate reductase, seedling isozyme (EC:1.6.5.4)
Short name:
MDAR seedling
Alternative name(s):
Ascorbate free radical reductase seedling
Short name:
AFR reductase seedling
OrganismiCucumis sativus (Cucumber)Imported
Taxonomic identifieri3659 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Monodehydroascorbate reductase, seedling isozymePRO_0000209140Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ42711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

KOiK08232.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

Q42711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADETFKYVI LGGGVAAGYA AREFVKQGLN PGELAIISKE AVAPYERPAL
60 70 80 90 100
SKAYLFPESP ARLPGFHVCV GSGGERLLPD WYKEKGIELI LSTEIVEADL
110 120 130 140 150
PAKRLRSAHG KIYNYQTLII ATGSTVIKLS DFGVQGADAK NIFYLREIDD
160 170 180 190 200
ADQLVEAIKA KENGKVVVVG GGYIGLELGA ALRINNFDVS MVYPEPWCMP
210 220 230 240 250
RLFTPEIAAF YEGYYAQKGI TIIKGTVAVG FTVDTNGEVK EVKLKDGRVL
260 270 280 290 300
EADIVVVGVG ARPLTSLFKG QIVEEKGGIK TDEFFKTSVP DVYAVGDVAT
310 320 330 340 350
FPLKLYNELR RVEHVDHSRK SAEQAVKAIK ASEEGKAIEE YDYLPYFYSR
360 370 380 390 400
SFDLSWQFYG DNVGDAVLFG DNSPDSATHK FGSYWIKDGK VVGAFLESGS
410 420 430
PEENKAIAKV ARIQPSVESS DLLLKEGISF ASKV
Length:434
Mass (Da):47,416
Last modified:November 1, 1996 - v1
Checksum:i302DA61F8C3E4E23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26392 mRNA. Translation: BAA05408.1.
PIRiJU0182.
RefSeqiNP_001267683.1. NM_001280754.1.

Genome annotation databases

GeneIDi101210277.
KEGGicsv:101210277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26392 mRNA. Translation: BAA05408.1.
PIRiJU0182.
RefSeqiNP_001267683.1. NM_001280754.1.

3D structure databases

ProteinModelPortaliQ42711.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101210277.
KEGGicsv:101210277.

Phylogenomic databases

KOiK08232.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMDARS_CUCSA
AccessioniPrimary (citable) accession number: Q42711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. 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.