Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

D-galacturonate reductase

Gene

GALUR

Organism
Fragaria ananassa (Strawberry)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in ascorbic acid (vitamin C) biosynthesis.2 Publications

Catalytic activityi

L-galactonate + NADP+ = D-galacturonate + NADPH.1 Publication

Cofactori

NADP+1 Publication

Pathwayi: L-ascorbate biosynthesis

This protein is involved in the pathway L-ascorbate biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway L-ascorbate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581Proton donorBy similarity
Binding sitei121 – 1211SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi216 – 27560NADPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00132.

Names & Taxonomyi

Protein namesi
Recommended name:
D-galacturonate reductase (EC:1.1.1.365)
Short name:
FaGalUR
Alternative name(s):
Aldo-keto reductase 2
Gene namesi
Name:GALUR
Synonyms:AKR2
OrganismiFragaria ananassa (Strawberry)
Taxonomic identifieri3747 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeRosoideaePotentilleaeFragariinaeFragaria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319D-galacturonate reductasePRO_0000425862Add
BLAST

Expressioni

Tissue specificityi

Expressed specifically in the receptacle tissue of the fruit.1 Publication

Developmental stagei

Up-regulated during ripening, with a highest expression in fully mature red fruit.2 Publications

Structurei

3D structure databases

ProteinModelPortaliO49133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

KOiK19642.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O49133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVPSVTLS SCGDDIQTMP VIGMGTSSYP RADPETAKAA ILEAIRAGYR
60 70 80 90 100
HFDTAAAYGS EKDLGEAIAE ALRLQLIKSR DELFITTKLW ASFAEKDLVL
110 120 130 140 150
PSIKASLSNL QVEYIDMYII HWPFKLGKEV RTMPVERDLV QPLDIKSVWE
160 170 180 190 200
AMEECKKLGL ARGIGVSNFT SSMLEELLSF AEIPPAVNQL EMNPAWQLKK
210 220 230 240 250
LRDFCKAKGI HVTAYSPLGA ARTKWGDDRV LGSDIIEEIA QAKGKSTAQI
260 270 280 290 300
SLRWVYEQGV SIVTKSYNKE RMRQNLDIFD FCLTEEELEK MSHLPQRKGV
310
TFASILGPHD IVLEVDEEL
Length:319
Mass (Da):35,669
Last modified:June 1, 1998 - v1
Checksum:iABE8523B6E383349
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039182 mRNA. Translation: AAB97005.1.

Genome annotation databases

KEGGiag:AAB97005.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039182 mRNA. Translation: AAB97005.1.

3D structure databases

ProteinModelPortaliO49133.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAB97005.

Phylogenomic databases

KOiK19642.

Enzyme and pathway databases

UniPathwayiUPA00132.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Engineering increased vitamin C levels in plants by overexpression of a D-galacturonic acid reductase."
    Agius F., Gonzalez-Lamothe R., Caballero J.L., Munoz-Blanco J., Botella M.A., Valpuesta V.
    Nat. Biotechnol. 21:177-181(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: cv. Chandler.
  2. Cited for: FUNCTION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiGALUR_FRAAN
AccessioniPrimary (citable) accession number: O49133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: June 1, 1998
Last modified: April 13, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.