Reviewed, UniProtKB/Swiss-Prot P38115 (ARA1_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.4
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
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Ref.3 Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.3 Inferred from direct assay. Source: SGD
Molecular function	D-arabinose 1-dehydrogenase [NAD(P)+] activity Ref.3 Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-2790,EBI-2790

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.5 Ref.6
	Modified residue	294	1	Phosphoserine Ref.6
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)
	P38115-1 [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: 2005616] [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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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: 9920381] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 7-20.
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151, MASS SPECTROMETRY.
[6]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151 AND SER-294, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M95580 Genomic DNA. Translation: AAA35037.1. Z36018 Genomic DNA. Translation: CAA85107.1.
PIR	S46020.
RefSeq	NP_009707.1.
3D structure databases
HSSP	HSSP built from PDB template 1HW6 based on UniProtKB P06632.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4926N.
IntAct	P38115. 4 interactions.
Proteomic databases
PeptideAtlas	P38115.
Genome annotation databases
Ensembl	YBR149W. Saccharomyces cerevisiae. [Contig view]
GeneID	852446.
GenomeReviews	Gene locus YBR149W in contig Y13134_GR.
KEGG	sce:YBR149W.
NMPDR	fig|4932.3.peg.413.
Organism-specific databases
CYGD	YBR149w.
SGD	S000000353. ARA1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38115.
OMA	P38115. LQHWPLC.
Enzyme and pathway databases
BRENDA	1.1.1.117. 250.
Gene expression databases
GermOnline	YBR149W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
ProDom	PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	971354.

Entry information

Entry name

ARA1_YEAST

Accession

Primary (citable) accession number: P38115

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)