NUCLEOTIDE SEQUENCE [MRNA], AND ENZYME ACTIVITY.
DOI=10.1021/bi025529i; PubMed=12009906 [NCBI, ExPASy, EBI, Israel, Japan]
Richard P., Putkonen M., Vaeaenaenen R., Londesborough J., Penttilae M.;
"The missing link in the fungal L-arabinose catabolic pathway, identification of the L-xylulose reductase gene.";
Biochemistry 41:6432-6437(2002).

Comments

FUNCTION: Catalyzes the NADPH-dependent reduction of L-xylulose, D-xylulose, D-fructose, and L-sorbose, with the highest affinity for L-xylulose.
CATALYTIC ACTIVITY: Xylitol + NADP⁺ = L-xylulose + NADPH.
PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungi route): step 3/5 .
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) 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

AF375616; AAM20896.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q9ZFY9; 1FK8. [HSSP ENTRY / PDB]

ModBase

Q8NK50.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13194; -.

Ontologies

GO:0050038;	Molecular function: L-xylulose reductase activity (inferred from electronic annotation from EC).
GO:0042732;	Biological process: D-xylose metabolic process (inferred from electronic annotation from UniProtKB-KW).
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; FALSE_NEG.

Other

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

Keywords

Carbohydrate metabolism; NADP; Oxidoreductase; Xylose metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 266`	`266`	`L-xylulose reductase.`	`PRO_0000054558`
`NP_BIND`	`23 53`	`31`	`NADP (By similarity).`
`ACT_SITE`	`174 174`		`Proton acceptor (By similarity).`
`ACT_SITE`	`178 178`		`By similarity.`
`BINDING`	`159 159`		`Substrate (By similarity).`

Sequence information

Length: 266 AA [This is the length of the unprocessed precursor]

Molecular weight: 28478 Da [This is the MW of the unprocessed precursor]

CRC64: 1CF56334DA86F109 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPQPVPTANR LLDLFSLKGK VVVVTGASGP RGMGIEAARG CAEMGADLAI TYSSRKEGAE 

        70         80         90        100        110        120 
KNAEELTKEY GVKVKVYKVN QSDYNDVERF VNQVVSDFGK IDAFIANAGA TANSGVVDGS 

       130        140        150        160        170        180 
ASDWDHVIQV DLSGTAYCAK AVGAHFKKQG HGSLVITASM SGHVANYPQE QTSYNVAKAG 

       190        200        210        220        230        240 
CIHLARSLAN EWRDFARVNS ISPGYIDTGL SDFIDEKTQE LWRSMIPMGR NGDAKELKGA 

       250        260 
YVYLVSDASS YTTGADIVID GGYTTR

Q8NK50 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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