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Protein

D-arabinose dehydrogenase [NAD(P)+] heavy chain

Gene

ARA1

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

Functioni

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

Catalytic activityi

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

pH dependencei

Optimum pH is 10.0.

Temperature dependencei

Optimum temperature is about 30 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711Proton donorBy similarity
Sitei100 – 1001Lowers pKa of active site TyrBy similarity
Binding sitei131 – 1311SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi241 – 29555NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. D-arabinose 1-dehydrogenase [NAD(P)+] activity Source: SGD

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
D-arabinose dehydrogenase [NAD(P)+] heavy chain (EC:1.1.1.117)
Alternative name(s):
AKR3C
Gene namesi
Name:ARA1
Ordered Locus Names:YBR149W
ORF Names:YBR1127
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBR149w.
EuPathDBiFungiDB:YBR149W.
SGDiS000000353. ARA1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344D-arabinose dehydrogenase [NAD(P)+] heavy chainPRO_0000124610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38115.
PaxDbiP38115.
PeptideAtlasiP38115.

Expressioni

Gene expression databases

GenevestigatoriP38115.

Interactioni

Subunit structurei

Heterodimer of a heavy chain and a light chain.

Protein-protein interaction databases

BioGridi32848. 23 interactions.
DIPiDIP-4926N.
MINTiMINT-521486.
STRINGi4932.YBR149W.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 223Combined sources
Beta strandi23 – 264Combined sources
Beta strandi32 – 365Combined sources
Helixi44 – 496Combined sources
Helixi50 – 5910Combined sources
Beta strandi64 – 663Combined sources
Helixi69 – 713Combined sources
Helixi74 – 8613Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 1016Combined sources
Helixi103 – 1053Combined sources
Helixi109 – 12012Combined sources
Beta strandi126 – 1305Combined sources
Helixi167 – 17913Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi189 – 1935Combined sources
Helixi196 – 20510Combined sources
Beta strandi211 – 2166Combined sources
Helixi224 – 23310Combined sources
Beta strandi236 – 2416Combined sources
Helixi249 – 2524Combined sources
Helixi254 – 2629Combined sources
Helixi267 – 27711Combined sources
Helixi289 – 2946Combined sources
Helixi303 – 31513Combined sources
Helixi324 – 3263Combined sources
Helixi339 – 3413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IJCX-ray2.10A/B1-344[»]
4IJRX-ray2.00A/C1-344[»]
ProteinModelPortaliP38115.
SMRiP38115. Positions 15-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00780000122778.
HOGENOMiHOG000250272.
InParanoidiP38115.
KOiK00063.
OrthoDBiEOG7WQ83S.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38115-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSVASTEN IVENMLHPKT TEIYFSLNNG VRIPALGLGT ANPHEKLAET
60 70 80 90 100
KQAVKAAIKA GYRHIDTAWA YETEPFVGEA IKELLEDGSI KREDLFITTK
110 120 130 140 150
VWPVLWDEVD RSLNESLKAL GLEYVDLLLQ HWPLCFEKIK DPKGISGLVK
160 170 180 190 200
TPVDDSGKTM YAADGDYLET YKQLEKIYLD PNDHRVRAIG VSNFSIEYLE
210 220 230 240 250
RLIKECRVKP TVNQVETHPH LPQMELRKFC FMHDILLTAY SPLGSHGAPN
260 270 280 290 300
LKIPLVKKLA EKYNVTGNDL LISYHIRQGT IVIPRSLNPV RISSSIEFAS
310 320 330 340
LTKDELQELN DFGEKYPVRF IDEPFAAILP EFTGNGPNLD NLKY
Length:344
Mass (Da):38,884
Last modified:October 1, 1994 - v1
Checksum:iF9B6D9333B18FEEC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 627AAIKAGY → LQSKLDN in AAA35037 (PubMed:2005616).Curated
Sequence conflicti71 – 733YET → SR in AAA35037 (PubMed:2005616).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95580 Genomic DNA. Translation: AAA35037.1.
Z36018 Genomic DNA. Translation: CAA85107.1.
BK006936 Genomic DNA. Translation: DAA07264.1.
PIRiS46020.
RefSeqiNP_009707.3. NM_001178497.3.

Genome annotation databases

EnsemblFungiiYBR149W; YBR149W; YBR149W.
GeneIDi852446.
KEGGisce:YBR149W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95580 Genomic DNA. Translation: AAA35037.1.
Z36018 Genomic DNA. Translation: CAA85107.1.
BK006936 Genomic DNA. Translation: DAA07264.1.
PIRiS46020.
RefSeqiNP_009707.3. NM_001178497.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IJCX-ray2.10A/B1-344[»]
4IJRX-ray2.00A/C1-344[»]
ProteinModelPortaliP38115.
SMRiP38115. Positions 15-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32848. 23 interactions.
DIPiDIP-4926N.
MINTiMINT-521486.
STRINGi4932.YBR149W.

Proteomic databases

MaxQBiP38115.
PaxDbiP38115.
PeptideAtlasiP38115.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR149W; YBR149W; YBR149W.
GeneIDi852446.
KEGGisce:YBR149W.

Organism-specific databases

CYGDiYBR149w.
EuPathDBiFungiDB:YBR149W.
SGDiS000000353. ARA1.

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00780000122778.
HOGENOMiHOG000250272.
InParanoidiP38115.
KOiK00063.
OrthoDBiEOG7WQ83S.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi971354.
PROiP38115.

Gene expression databases

GenevestigatoriP38115.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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].

Entry informationi

Entry nameiARA1_YEAST
AccessioniPrimary (citable) accession number: P38115
Secondary accession number(s): D6VQE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 29, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 30200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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