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UniProtKB/Swiss-Prot entry P23901


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDR_HORVU
Primary accession number P23901
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 52)
Name and origin of the protein
Protein name Aldose reductase
Synonyms AR
EC 1.1.1.21
Aldehyde reductase
Gene name None
From
Hordeum vulgare (Barley) [TaxID: 4513] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Triticeae; Hordeum.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Aura;
PubMed=1827067 [NCBI, ExPASy, EBI, Israel, Japan]
Bartels D., Engelhardt K., Roncarati R., Schneider K., Rotter M., Salamini F.;
"An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein.";
EMBO J. 10:1037-1043(1991).
[2]
X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 2-320.
DOI=10.1002/prot.21996; PubMed=18300247 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.G., Pedersen L., Christensen C.L., Olsen O., Henriksen A.;
"Barley aldose reductase: structure, cofactor binding, and substrate recognition in the aldo/keto reductase 4C family.";
Proteins 71:1572-1581(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X57526; CAA40747.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15024; S15024.
3D structure databases
PDB
2BGQ; X-ray; 2.50 A; A=2-320.[ExPASy / RCSB / EBI]
2BGS; X-ray; 1.64 A; A=2-320.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BGQ; -.
2BGS; -.
SMR P23901; 13-320.
ModBase P23901.
Organism-specific databases
Gramene P23901; -.
Ontologies
GO
GO:0004032; Molecular function: aldehyde reductase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00069; ALDKETRDTASE.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.
ProtoNet P23901.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; NADP; Oxidoreductase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   320  320     Aldose reductase. PRO_0000124628
NP_BIND   215   269  55     NADP (By similarity). 
ACT_SITE   60    60        Proton donor (By similarity). 
BINDING   121   121        Substrate (By similarity). 
SITE   88    88  1     Lowers pKa of active site Tyr (By similarity). 
Sequence information
Length: 320 AA [This is the length of the unprocessed precursor] Molecular weight: 35807 Da [This is the MW of the unprocessed precursor] CRC64: 5AA72C021E9A93C0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASAKATMGQ GEQDHFVLKS GHAMPAVGLG TWRAGSDTAH SVRTAITEAG YRHVDTAAEY 

        70         80         90        100        110        120 
GVEKEVGKGL KAAMEAGIDR KDLFVTSKIW CTNLAPERVR PALENTLKDL QLDYIDLYHI 

       130        140        150        160        170        180 
HWPFRLKDGA HMPPEAGEVL EFDMEGVWKE MENLVKDGLV KDIGVCNYTV TKLNRLLRSA 

       190        200        210        220        230        240 
KIPPAVCQME MHPGWKNDKI FEACKKHGIH VTAYSPLGSS EKNLAHDPVV EKVANKLNKT 

       250        260        270        280        290        300 
PGQVLIKWAL QRGTSVIPKS SKDERIKENI QVFGWEIPEE DFKVLCSIKD EKRVLTGEEL 

       310        320 
FVNKTHGPYR SAADVWDHEN 

P23901 in FASTA format

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