P38115 (ARA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular carbohydrate metabolic process Inferred from direct assay Ref.4. Source: SGD
Cellular_component	cytosol Inferred from direct assay Ref.4. Source: SGD
Molecular_function	D-arabinose 1-dehydrogenase [NAD(P)+] activity Inferred from direct assay Ref.4. Source: SGD alditol:NADP+ 1-oxidoreductase activity Inferred from sequence or structural similarity PubMed 11306085. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	D-arabinose dehydrogenase [NAD(P)+] heavy chain		PRO_0000124610
Regions
	Nucleotide binding	241 – 295	55	NADP By similarity
Sites
	Active site	71	1	Proton donor By similarity
	Binding site	131	1	Substrate By similarity
	Site	100	1	Lowers pKa of active site Tyr By similarity
Amino acid modifications
	Modified residue	151	1	Phosphothreonine Ref.6 Ref.7
	Modified residue	294	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	56 – 62	7	AAIKAGY → LQSKLDN in AAA35037. Ref.1
	Sequence conflict	71 – 73	3	YET → SR in AAA35037. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38115 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: F9B6D9333B18FEEC	FASTA	344	38,884
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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 AND SER-294, MASS SPECTROMETRY.
+	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.
PIR	S46020.
RefSeq	NP_009707.3. NM_001178497.3.
3D structure databases
ProteinModelPortal	P38115.
SMR	P38115. Positions 27-337.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4926N.
IntAct	P38115. 1 interaction.
MINT	MINT-521486.
STRING	4932.YBR149W.
Proteomic databases
PaxDb	P38115.
PeptideAtlas	P38115.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR149W; YBR149W; YBR149W.
GeneID	852446.
KEGG	sce:YBR149W. sce:YBR153W.
Organism-specific databases
CYGD	YBR149w.
SGD	S000000353. ARA1.
Phylogenomic databases
eggNOG	COG0656.
GeneTree	ENSGT00600000084576.
HOGENOM	HOG000250272.
KO	K00063. K14654.
OMA	LQHWPLC.
OrthoDB	EOG4PCF24.
Gene expression databases
Genevestigator	P38115.
GermOnline	YBR149W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.20.20.100. 1 hit.
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. IPR020471. Aldo/keto_reductase_subgr. IPR023210. NADP_OxRdtase_dom. [Graphical view]
PANTHER	PTHR11732. PTHR11732. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
PIRSF	PIRSF000097. AKR. 1 hit.
PRINTS	PR00069. ALDKETRDTASE.
SUPFAM	SSF51430. Aldo/ket_red. 1 hit.
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971354.

Entry information

Entry name

ARA1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program