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Protein

Aldehyde reductase 2

Gene
N/A
Organism
Sporidiobolus salmonicolor (Sporobolomyces salmonicolor)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the asymmetric reduction of o-substituted aliphatic and aromatic aldehydes and ketones to an S-enantiomer. Reduces ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.2 Publications

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.2 Publications

Enzyme regulationi

Inhibited by quercetin and diphenylhydantoin.1 Publication

pH dependencei

Optimum pH is 5.5.

Temperature dependencei

Optimum temperature is 40 degrees Celsius.

GO - Molecular functioni

  • alcohol dehydrogenase (NADP+) activity Source: UniProtKB
  • coenzyme binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde reductase 2 (EC:1.1.1.2)
Alternative name(s):
Aldehyde reductase II
Short name:
ARII
OrganismiSporidiobolus salmonicolor (Sporobolomyces salmonicolor)Imported
Taxonomic identifieri5005 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaMicrobotryomycetesSporidiobolalesSporidiobolaceaeSporidiobolus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191G → A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity. 1 Publication
Mutagenesisi22 – 221G → A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity. 1 Publication
Mutagenesisi25 – 251A → G: Only active when NADPH is replaced by NADH. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 343342Aldehyde reductase 2PRO_0000215575Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
343
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 185Combined sources
Turni19 – 213Combined sources
Helixi23 – 3412Combined sources
Beta strandi38 – 458Combined sources
Helixi46 – 5914Combined sources
Turni61 – 633Combined sources
Beta strandi64 – 685Combined sources
Turni75 – 8410Combined sources
Beta strandi86 – 905Combined sources
Helixi101 – 12020Combined sources
Beta strandi127 – 1315Combined sources
Helixi134 – 1363Combined sources
Helixi156 – 1649Combined sources
Helixi172 – 19524Combined sources
Beta strandi198 – 21013Combined sources
Turni216 – 2183Combined sources
Helixi222 – 23110Combined sources
Helixi237 – 2404Combined sources
Beta strandi244 – 2496Combined sources
Helixi250 – 26213Combined sources
Beta strandi270 – 2734Combined sources
Beta strandi276 – 2783Combined sources
Helixi280 – 29011Combined sources
Helixi313 – 3219Combined sources
Helixi330 – 3389Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJMX-ray2.00A/B2-343[»]
1Y1PX-ray1.60A/B2-343[»]
1ZZEX-ray1.80A/B2-343[»]
ProteinModelPortaliQ9UUN9.
SMRiQ9UUN9. Positions 2-343.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UUN9.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UUN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIDNAVLP EGSLVLVTGA NGFVASHVVE QLLEHGYKVR GTARSASKLA
60 70 80 90 100
NLQKRWDAKY PGRFETAVVE DMLKQGAYDE VIKGAAGVAH IASVVSFSNK
110 120 130 140 150
YDEVVTPAIG GTLNALRAAA ATPSVKRFVL TSSTVSALIP KPNVEGIYLD
160 170 180 190 200
EKSWNLESID KAKTLPESDP QKSLWVYAAS KTEAELAAWK FMDENKPHFT
210 220 230 240 250
LNAVLPNYTI GTIFDPETQS GSTSGWMMSL FNGEVSPALA LMPPQYYVSA
260 270 280 290 300
VDIGLLHLGC LVLPQIERRR VYGTAGTFDW NTVLATFRKL YPSKTFPADF
310 320 330 340
PDQGQDLSKF DTAPSLEILK SLGRPGWRSI EESIKDLVGS ETA
Length:343
Mass (Da):37,318
Last modified:January 23, 2007 - v3
Checksum:iC6CAAD9DB32E05C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160799 Genomic DNA. Translation: AAF15999.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160799 Genomic DNA. Translation: AAF15999.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJMX-ray2.00A/B2-343[»]
1Y1PX-ray1.60A/B2-343[»]
1ZZEX-ray1.80A/B2-343[»]
ProteinModelPortaliQ9UUN9.
SMRiQ9UUN9. Positions 2-343.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UUN9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiALD2_SPOSA
AccessioniPrimary (citable) accession number: Q9UUN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.