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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)DescriptionActionsGraphical viewLength
Mutagenesisi19G → A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity. 1 Publication1
Mutagenesisi22G → A: Results in loss of substrate inhibition and of NADPH-dependent reductase activity. 1 Publication1
Mutagenesisi25A → G: Only active when NADPH is replaced by NADH. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002155752 – 343Aldehyde reductase 2Add BLAST342

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1343
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 18Combined sources5
Turni19 – 21Combined sources3
Helixi23 – 34Combined sources12
Beta strandi38 – 45Combined sources8
Helixi46 – 59Combined sources14
Turni61 – 63Combined sources3
Beta strandi64 – 68Combined sources5
Turni75 – 84Combined sources10
Beta strandi86 – 90Combined sources5
Helixi101 – 120Combined sources20
Beta strandi127 – 131Combined sources5
Helixi134 – 136Combined sources3
Helixi156 – 164Combined sources9
Helixi172 – 195Combined sources24
Beta strandi198 – 210Combined sources13
Turni216 – 218Combined sources3
Helixi222 – 231Combined sources10
Helixi237 – 240Combined sources4
Beta strandi244 – 249Combined sources6
Helixi250 – 262Combined sources13
Beta strandi270 – 273Combined sources4
Beta strandi276 – 278Combined sources3
Helixi280 – 290Combined sources11
Helixi313 – 321Combined sources9
Helixi330 – 338Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9UUN9.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UJMX-ray2.00A/B2-343[»]
1Y1PX-ray1.60A/B2-343[»]
1ZZEX-ray1.80A/B2-343[»]
ProteinModelPortaliQ9UUN9.
SMRiQ9UUN9.
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.
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: November 30, 2016
This is version 72 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.