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P38115 (ARA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-arabinose dehydrogenase [NAD(P)+] heavy chain

EC=1.1.1.117
Alternative name(s):
AKR3C
Gene names
Name:ARA1
Ordered Locus Names:YBR149W
ORF Names:YBR1127
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose and L-galactose in the presence of NADP+.

Catalytic activity

D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H.

Subunit structure

Heterodimer of a heavy chain and a light chain.

Subcellular location

Cytoplasm.

Miscellaneous

Present with 30200 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the aldo/keto reductase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 10.0.

Temperature dependence:

Optimum temperature is about 30 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344D-arabinose dehydrogenase [NAD(P)+] heavy chain
PRO_0000124610

Regions

Nucleotide binding241 – 29555NADP By similarity

Sites

Active site711Proton donor By similarity
Binding site1311Substrate By similarity
Site1001Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue1511Phosphothreonine Ref.6 Ref.7

Experimental info

Sequence conflict56 – 627AAIKAGY → LQSKLDN in AAA35037. Ref.1
Sequence conflict71 – 733YET → SR in AAA35037. Ref.1

Secondary structure

..................................................... 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38115 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F9B6D9333B18FEEC

FASTA34438,884
        10         20         30         40         50         60 
MSSSVASTEN IVENMLHPKT TEIYFSLNNG VRIPALGLGT ANPHEKLAET KQAVKAAIKA 

        70         80         90        100        110        120 
GYRHIDTAWA YETEPFVGEA IKELLEDGSI KREDLFITTK VWPVLWDEVD RSLNESLKAL 

       130        140        150        160        170        180 
GLEYVDLLLQ HWPLCFEKIK DPKGISGLVK TPVDDSGKTM YAADGDYLET YKQLEKIYLD 

       190        200        210        220        230        240 
PNDHRVRAIG VSNFSIEYLE RLIKECRVKP TVNQVETHPH LPQMELRKFC FMHDILLTAY 

       250        260        270        280        290        300 
SPLGSHGAPN LKIPLVKKLA EKYNVTGNDL LISYHIRQGT IVIPRSLNPV RISSSIEFAS 

       310        320        330        340 
LTKDELQELN DFGEKYPVRF IDEPFAAILP EFTGNGPNLD NLKY 

« Hide

References

« Hide 'large scale' references
[1]"A widely distributed 'CAT' family of repetitive DNA sequences."
Martinez-Soriano J.P., Wong W.M., van Ryk D.I., Nazar R.N.
J. Mol. Biol. 217:629-635(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"D-arabinose dehydrogenase and its gene from Saccharomyces cerevisiae."
Kim S.T., Huh W.K., Lee B.H., Kang S.O.
Biochim. Biophys. Acta 1429:29-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 7-20.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95580 Genomic DNA. Translation: AAA35037.1.
Z36018 Genomic DNA. Translation: CAA85107.1.
BK006936 Genomic DNA. Translation: DAA07264.1.
PIRS46020.
RefSeqNP_009707.3. NM_001178497.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IJCX-ray2.10A/B1-344[»]
4IJRX-ray2.00A/C1-344[»]
ProteinModelPortalP38115.
SMRP38115. Positions 15-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32848. 21 interactions.
DIPDIP-4926N.
MINTMINT-521486.
STRING4932.YBR149W.

Proteomic databases

MaxQBP38115.
PaxDbP38115.
PeptideAtlasP38115.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR149W; YBR149W; YBR149W.
GeneID852446.
KEGGsce:YBR149W.

Organism-specific databases

CYGDYBR149w.
SGDS000000353. ARA1.

Phylogenomic databases

eggNOGCOG0656.
GeneTreeENSGT00750000117803.
HOGENOMHOG000250272.
KOK00063.
OrthoDBEOG7WQ83S.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER3O-32366.
MetaCyc:MONOMER3O-32367.
YEAST:MONOMER3O-32366.
YEAST:MONOMER3O-32367.

Gene expression databases

GenevestigatorP38115.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971354.

Entry information

Entry nameARA1_YEAST
AccessionPrimary (citable) accession number: P38115
Secondary accession number(s): D6VQE4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references