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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)DescriptionActionsGraphical viewLength
Active sitei71Proton donorBy similarity1
Sitei100Lowers pKa of active site TyrBy similarity1
Binding sitei131SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi241 – 295NADPBy similarityAdd BLAST55

GO - Molecular functioni

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

GO - Biological processi

  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR149W.
SGDiS000000353. ARA1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001246101 – 344D-arabinose dehydrogenase [NAD(P)+] heavy chainAdd BLAST344

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei151PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38115.
PRIDEiP38115.

PTM databases

iPTMnetiP38115.

Interactioni

Subunit structurei

Heterodimer of a heavy chain and a light chain.

Protein-protein interaction databases

BioGridi32848. 22 interactors.
DIPiDIP-4926N.
MINTiMINT-521486.

Structurei

Secondary structure

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 22Combined sources3
Beta strandi23 – 26Combined sources4
Beta strandi32 – 36Combined sources5
Helixi44 – 49Combined sources6
Helixi50 – 59Combined sources10
Beta strandi64 – 66Combined sources3
Helixi69 – 71Combined sources3
Helixi74 – 86Combined sources13
Helixi92 – 94Combined sources3
Beta strandi96 – 101Combined sources6
Helixi103 – 105Combined sources3
Helixi109 – 120Combined sources12
Beta strandi126 – 130Combined sources5
Helixi167 – 179Combined sources13
Beta strandi185 – 187Combined sources3
Beta strandi189 – 193Combined sources5
Helixi196 – 205Combined sources10
Beta strandi211 – 216Combined sources6
Helixi224 – 233Combined sources10
Beta strandi236 – 241Combined sources6
Helixi249 – 252Combined sources4
Helixi254 – 262Combined sources9
Helixi267 – 277Combined sources11
Helixi289 – 294Combined sources6
Helixi303 – 315Combined sources13
Helixi324 – 326Combined sources3
Helixi339 – 341Combined sources3

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

GeneTreeiENSGT00850000132445.
HOGENOMiHOG000250272.
InParanoidiP38115.
KOiK00063.
OMAiKIFNGDQ.
OrthoDBiEOG092C324N.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti56 – 62AAIKAGY → LQSKLDN in AAA35037 (PubMed:2005616).Curated7
Sequence conflicti71 – 73YET → SR in AAA35037 (PubMed:2005616).Curated3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IJCX-ray2.10A/B1-344[»]
4IJRX-ray2.00A/C1-344[»]
ProteinModelPortaliP38115.
SMRiP38115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32848. 22 interactors.
DIPiDIP-4926N.
MINTiMINT-521486.

PTM databases

iPTMnetiP38115.

Proteomic databases

MaxQBiP38115.
PRIDEiP38115.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YBR149W.
SGDiS000000353. ARA1.

Phylogenomic databases

GeneTreeiENSGT00850000132445.
HOGENOMiHOG000250272.
InParanoidiP38115.
KOiK00063.
OMAiKIFNGDQ.
OrthoDBiEOG092C324N.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP38115.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
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...

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: November 2, 2016
This is version 160 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

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.