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UniProtKB/Swiss-Prot entry P50167

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARDH_PICST
Primary accession number P50167
Secondary accession number A3LUR3
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
Name and origin of the protein
Protein name D-arabinitol 2-dehydrogenase [ribulose-forming]
Synonyms ARDH
EC 1.1.1.250
Gene name
Name: ARDH
Synonyms: ARD2
ORFNames: PICST_65696
From
Pichia stipitis (Yeast) [TaxID: 4924] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545;
DOI=10.1002/yea.320110906; PubMed=7483848 [NCBI, ExPASy, EBI, Israel, Japan]
Hallborn J., Walfridsson M., Penttilae M., Keraenen S., Hahn-Haegerdal B.;
"A short-chain dehydrogenase gene from Pichia stipitis having D-arabinitol dehydrogenase activity.";
Yeast 11:839-847(1995).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545;
DOI=10.1038/nbt1290; PubMed=17334359 [NCBI, ExPASy, EBI, Israel, Japan]
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.;
"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis.";
Nat. Biotechnol. 25:319-326(2007).
Comments
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
Z46866; CAA86939.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000499; ABN67006.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S57351; S57351.
RefSeq XP_001385035.1; -.
3D structure databases
HSSP Q9ZFY9; 1FK8. [HSSP ENTRY / PDB]
ModBase P50167.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0047038; Molecular function: D-arabinitol 2-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
Genome annotation databases
GeneID 4839199; -.
KEGG pic:PICST_65696; -.
Other
ProtoNet P50167.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   278  278     D-arabinitol 2-dehydrogenase [ribulose-forming]. PRO_0000054519
NP_BIND   22    44  23     NAD (By similarity). 
ACT_SITE   181   181        Proton acceptor (By similarity). 
BINDING   166   166        Substrate (By similarity). 
Sequence information
Length: 278 AA [This is the length of the unprocessed precursor] Molecular weight: 30003 Da [This is the MW of the unprocessed precursor] CRC64: 36869165F23964F6 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDYSYANVVP NFRLDGRLAI ITGGSGGLAA VISRALLAQG ADVALIDMNL ERTKSAAKEV 

        70         80         90        100        110        120 
LGWGEETLKG EHASAIGQVS AWSCNIGDAE AVDATFSSIN EHHGKIADLL INTAGYCENF 

       130        140        150        160        170        180 
PAETYPATNA ESIMKVNGLG SFYVSQSFAR PLIQNNLRGS IILIGSMSGT IVNDPQPQCM 

       190        200        210        220        230        240 
YNMSKAGVIH LVRSLACEWA KYNIRVNTLS PGYILTPLTR NVISGHTEMK EAWESKIPMK 

       250        260        270 
RMAEPKEFVG SILYLASETA SSYTTGHNLV VDGGYECW
P50167 in FASTA format

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