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Identification
HMDB Protein ID HMDBP00306
Secondary Accession Numbers
  • 5541
  • HMDBP04301
Name L-xylulose reductase
Synonyms
  1. Carbonyl reductase II
  2. Dicarbonyl/L-xylulose reductase
  3. Kidney dicarbonyl reductase
  4. Sperm surface protein P34H
  5. XR
  6. kiDCR
Gene Name DCXR
Protein Type Enzyme
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
Pathways
  • Pentose and glucuronate interconversions
Reactions
D-Xylitol + NADP → L-Xylulose + NADPH details
D-Xylitol + NADP → L-Xylulose + NADPH + Hydrogen Ion details
GO Classification
Biological Process
D-xylose metabolic process
NADP metabolic process
xylulose metabolic process
glucose metabolic process
protein homotetramerization
Cellular Component
brush border
microvillus
membrane
Function
binding
catalytic activity
oxidoreductase activity
Molecular Function
L-xylulose reductase (NADP+) activity
oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor
nucleotide binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Peripheral membrane protein
  2. Membrane
Gene Properties
Chromosome Location 17
Locus 17q25.3
SNPs DCXR
Gene Sequence
>735 bp
ATGGAGCTGTTCCTCGCGGGCCGCCGGGTGCTGGTCACCGGGGCAGGCAAAGGTATAGGG
CGCGGCACGGTCCAGGCGCTGCACGCGACGGGCGCGCGGGTGGTGGCTGTGAGCCGGACT
CAGGCGGATCTTGACAGCCTTGTCCGCGAGTGCCCGGGGATAGAACCCGTGTGCGTGGAC
CTGGGTGACTGGGAGGCCACCGAGCGGGCGCTGGGCAGCGTGGGCCCCGTGGACCTGCTG
GTGAACAACGCCGCTGTCGCCCTGCTGCAGCCCTTCCTGGAGGTCACCAAGGAGGCCTTT
GACAGATCCTTTGAGGTGAACCTGCGTGCGGTCATCCAGGTGTCGCAGATTGTGGCCAGG
GGCTTAATAGCCCGGGGAGTCCCAGGGGCCATCGTGAATGTCTCCAGCCAGTGCTCCCAG
CGGGCAGTAACTAACCATAGCGTCTACTGCTCCACCAAGGGTGCCCTGGACATGCTGACC
AAGGTGATGGCCCTAGAGCTCGGGCCCCACAAGATCCGAGTGAATGCAGTAAACCCCACA
GTGGTGATGACGTCCATGGGCCAGGCCACCTGGAGTGACCCCCACAAGGCCAAGACTATG
CTGAACCGAATCCCACTTGGCAAGTTTGCTGAGGTAGAGCACGTGGTGAACGCCATCCTC
TTTCTGCTGAGTGACCGAAGTGGCATGACCACGGGTTCCACTTTGCCGGTGGAAGGGGGC
TTCTGGGCCTGCTGA
Protein Properties
Number of Residues 244
Molecular Weight 25742.665
Theoretical pI 8.109
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>L-xylulose reductase
MELFLAGRRVLVTGAGKGIGRGTVQALHATGARVVAVSRTQADLDSLVRECPGIEPVCVD
LGDWEATERALGSVGPVDLLVNNAAVALLQPFLEVTKEAFDRSFEVNLRAVIQVSQIVAR
GLIARGVPGAIVNVSSQCSQRAVTNHSVYCSTKGALDMLTKVMALELGPHKIRVNAVNPT
VVMTSMGQATWSDPHKAKTMLNRIPLGKFAEVEHVVNAILFLLSDRSGMTTGSTLPVEGG
FWAC
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q7Z4W1
UniProtKB/Swiss-Prot Entry Name DCXR_HUMAN
PDB IDs
GenBank Gene ID AB013846
GeneCard ID DCXR
GenAtlas ID DCXR
HGNC ID HGNC:18985
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  4. Legare C, Gaudreault C, St-Jacques S, Sullivan R: P34H sperm protein is preferentially expressed by the human corpus epididymidis. Endocrinology. 1999 Jul;140(7):3318-27. [PubMed:10385429 ]
  5. Nakagawa J, Ishikura S, Asami J, Isaji T, Usami N, Hara A, Sakurai T, Tsuritani K, Oda K, Takahashi M, Yoshimoto M, Otsuka N, Kitamura K: Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney. J Biol Chem. 2002 May 17;277(20):17883-91. Epub 2002 Mar 6. [PubMed:11882650 ]
  6. Xia XY, Xu XF, Gao Y, Huang YF: [Molecular cloning of human sperm surface protein P34H gene and semi-quantitative analysis of its expression in testis and epididymidis]. Zhonghua Nan Ke Xue. 2003 Feb;9(1):24-7. [PubMed:12680326 ]
  7. El-Kabbani O, Chung RP, Ishikura S, Usami N, Nakagawa J, Hara A: Crystallization and preliminary crystallographic analysis of human L-xylulose reductase. Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1379-80. Epub 2002 Jul 20. [PubMed:12136162 ]
  8. El-Kabbani O, Ishikura S, Darmanin C, Carbone V, Chung RP, Usami N, Hara A: Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis. Proteins. 2004 May 15;55(3):724-32. [PubMed:15103634 ]