NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1016/j.febslet.2006.10.058; PubMed=17097644 [NCBI, ExPASy, EBI, Israel, Japan]
Amako K., Fujita K., Shimohata T.A., Hasegawa E., Kishimoto R., Goda K.;
"NAD+-specific D-arabinose dehydrogenase and its contribution to erythroascorbic acid production in Saccharomyces cerevisiae.";
FEBS Lett. 580:6428-6434(2006).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan]
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
Nature 387:90-93(1997).

Comments

CATALYTIC ACTIVITY: D-arabinose + NAD⁺ = D-arabinono-1,4-lactone + NADH.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.78 mM for D-arabinose;
INTERACTION:
P39940:RSP5; NbExp=1; IntAct=EBI-28073, EBI-16219;
P40318:SSM4; NbExp=1; IntAct=EBI-28073, EBI-18208;
SIMILARITY: Belongs to the aldo/keto reductase 2 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB237161; BAE93049.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48502; CAA88407.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S52890; S52890.

RefSeq

NP_013755.1; -.

3D structure databases

ModBase

Q04212.

Protein-protein interaction databases

DIP

DIP:4506N; -.

IntAct

Q04212; -.

Organism-specific databases

YMR041c; -.

S000004644; ARA2.

Gene expression databases

ArrayExpress

Q04212; -.

GermOnline

YMR041C; Saccharomyces cerevisiae.

Ontologies

GO:0045290;	Molecular function: D-arabinose 1-dehydrogenase [NAD(P)+] activity (inferred from direct assay from SGD).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0019853;	Biological process: L-ascorbic acid biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR001395; Aldo/ket_red.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.100; Aldo/ket_red; 1.

PANTHER

PTHR11732; Aldo/ket_red; 1.

Pfam

PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.

PRINTS

PR00069; ALDKETRDTASE.

ProDom

PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00798; ALDOKETO_REDUCTASE_1; FALSE_NEG.
PS00062; ALDOKETO_REDUCTASE_2; FALSE_NEG.
PS00063; ALDOKETO_REDUCTASE_3; FALSE_NEG.

BLOCKS

Q04212.

Genome annotation databases

Ensembl

YMR041C; Saccharomyces cerevisiae. [Contig view]

855057; -.

Z71257_GR; YMR041C.

sce:YMR041C; -.

fig|4932.3.peg.4802; -.

Phylogenomic databases

HOGENOM

Q04212; -.

Other

Q04212; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 335`	`335`	`D-arabinose 1-dehydrogenase.`	`PRO_0000070372`
`NP_BIND`	`221 287`	`67`	`NAD (Potential).`
`ACT_SITE`	`58 58`		`Proton donor (By similarity).`
`BINDING`	`124 124`		`Substrate (Potential).`
`SITE`	`86 86`	`1`	`Lowers pKa of active site Tyr (By similarity).`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 38220 Da [This is the MW of the unprocessed precursor]

CRC64: CC7FA464FFAE6ED7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVNEKVNPFD LASVSPLVLG GAILNQQYTD EPESIPLEDI IKYAFSHGIN AIDTSPYYGP 

        70         80         90        100        110        120 
SEVLYGRALS NLRNEFPRDT YFICTKVGRI GAEEFNYSRD FVRFSVHRSC ERLHTTYLDL 

       130        140        150        160        170        180 
VYLHDVEFVK FPDILEALKE LRTLKNKGVI KNFGISGYPI DFITWLAEYC STEESDIGSL 

       190        200        210        220        230        240 
DAVLSYCNLN LQNNKLLNFR ERLLRNAKLK MVCNASILSM SLLRSQETRQ FHPCSHELRE 

       250        260        270        280        290        300 
CASQAAKYCQ EQNVDLADLA TRYAISEWVG KGPVVLGVSS MEELKLALDN YEIVKSNGNR 

       310        320        330 
LSSKDGQLVE YIQKNIFKEH FNEEWSSGIP HPEMI

Q04212 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools