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Protein

NADPH-dependent aldehyde reductase ARI1

Gene

ARI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

NADPH-dependent aldehyde reductase involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion. Reduces commonly detected inhibitors in biomass conversion hydrolysates such as furfural, 5-hydroxymethylfurfural (HMF), cinnamic aldehyde, benzaldehyde, phenylacetaldehyde, and anisaldehyde.3 Publications

Cofactori

NADPH2 Publications

pH dependencei

Optimum pH is 7.0.1 Publication

Temperature dependencei

Optimum temperature is 25 degrees Celsius.1 Publication

GO - Molecular functioni

  • carbonyl reductase (NADPH) activity Source: SGD
  • coenzyme binding Source: InterPro
  • oxidoreductase activity Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciYEAST:G3O-30646-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH-dependent aldehyde reductase ARI1 (EC:1.1.1.-)
Gene namesi
Name:ARI1
Ordered Locus Names:YGL157W
ORF Names:G1857
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL157w.
EuPathDBiFungiDB:YGL157W.
SGDiS000003125. ARI1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347NADPH-dependent aldehyde reductase ARI1PRO_0000215578Add
BLAST

Proteomic databases

MaxQBiP53111.
PaxDbiP53111.
PeptideAtlasiP53111.

Expressioni

Inductioni

By furfural and 5-hydroxymethylfurfural (HMF).1 Publication

Interactioni

Protein-protein interaction databases

BioGridi33097. 12 interactions.
DIPiDIP-5112N.
IntActiP53111. 8 interactions.
MINTiMINT-513533.

Structurei

3D structure databases

ProteinModelPortaliP53111.
SMRiP53111. Positions 6-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00390000002618.
InParanoidiP53111.
OrthoDBiEOG77M8ZW.

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]

Sequencei

Sequence statusi: Complete.

P53111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTDTTVFVS GATGFIALHI MNDLLKAGYT VIGSGRSQEK NDGLLKKFNN
60 70 80 90 100
NPKLSMEIVE DIAAPNAFDE VFKKHGKEIK IVLHTASPFH FETTNFEKDL
110 120 130 140 150
LTPAVNGTKS ILEAIKKYAA DTVEKVIVTS STAALVTPTD MNKGDLVITE
160 170 180 190 200
ESWNKDTWDS CQANAVAAYC GSKKFAEKTA WEFLKENKSS VKFTLSTINP
210 220 230 240 250
GFVFGPQMFA DSLKHGINTS SGIVSELIHS KVGGEFYNYC GPFIDVRDVS
260 270 280 290 300
KAHLVAIEKP ECTGQRLVLS EGLFCCQEIV DILNEEFPQL KGKIATGEPA
310 320 330 340
TGPSFLEKNS CKFDNSKTKK LLGFQFYNLK DCIVDTAAQM LEVQNEA
Length:347
Mass (Da):38,083
Last modified:October 1, 1996 - v1
Checksum:i51035AD526E418AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48618 Genomic DNA. No translation available.
Z72679 Genomic DNA. Translation: CAA96869.1.
BK006941 Genomic DNA. Translation: DAA07955.1.
PIRiS60428.
RefSeqiNP_011358.3. NM_001181022.3.

Genome annotation databases

EnsemblFungiiYGL157W; YGL157W; YGL157W.
GeneIDi852720.
KEGGisce:YGL157W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48618 Genomic DNA. No translation available.
Z72679 Genomic DNA. Translation: CAA96869.1.
BK006941 Genomic DNA. Translation: DAA07955.1.
PIRiS60428.
RefSeqiNP_011358.3. NM_001181022.3.

3D structure databases

ProteinModelPortaliP53111.
SMRiP53111. Positions 6-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33097. 12 interactions.
DIPiDIP-5112N.
IntActiP53111. 8 interactions.
MINTiMINT-513533.

Proteomic databases

MaxQBiP53111.
PaxDbiP53111.
PeptideAtlasiP53111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL157W; YGL157W; YGL157W.
GeneIDi852720.
KEGGisce:YGL157W.

Organism-specific databases

CYGDiYGL157w.
EuPathDBiFungiDB:YGL157W.
SGDiS000003125. ARI1.

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00390000002618.
InParanoidiP53111.
OrthoDBiEOG77M8ZW.

Enzyme and pathway databases

BioCyciYEAST:G3O-30646-MONOMER.

Miscellaneous databases

NextBioi972099.
PROiP53111.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43."
    James C.M., Indge K.J., Oliver S.G.
    Yeast 11:1413-1419(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Efficient anaerobic whole cell stereoselective bioreduction with recombinant Saccharomyces cerevisiae."
    Katz M., Frejd T., Hahn-Hagerdal B., Gorwa-Grauslund M.F.
    Biotechnol. Bioeng. 84:573-582(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "A novel NADPH-dependent aldehyde reductase gene from Saccharomyces cerevisiae NRRL Y-12632 involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion."
    Liu Z.L., Moon J.
    Gene 446:1-10(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
  8. "Stereochemistry of furfural reduction by a Saccharomyces cerevisiae aldehyde reductase that contributes to in situ furfural detoxification."
    Bowman M.J., Jordan D.B., Vermillion K.E., Braker J.D., Moon J., Liu Z.L.
    Appl. Environ. Microbiol. 76:4926-4932(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.

Entry informationi

Entry nameiARI1_YEAST
AccessioniPrimary (citable) accession number: P53111
Secondary accession number(s): D6VTZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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 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.