DCXR_CAEEL
ID DCXR_CAEEL Reviewed; 251 AA.
AC Q21929; Q27GP8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=L-xylulose reductase {ECO:0000250|UniProtKB:Q7Z4W1};
DE Short=XR;
DE EC=1.1.1.10 {ECO:0000269|PubMed:21477590};
DE AltName: Full=Dicarbonyl/L-xylulose reductase {ECO:0000303|PubMed:21477590};
DE Short=DCXR {ECO:0000303|PubMed:21477590};
DE AltName: Full=Short-chain dehydrogenase 21 {ECO:0000312|WormBase:R11D1.11};
GN Name=dhs-21 {ECO:0000312|WormBase:R11D1.11};
GN ORFNames=R11D1.11 {ECO:0000312|WormBase:R11D1.11};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAA99897.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21300042; DOI=10.1016/j.cbi.2011.01.034;
RA Kisiela M., El-Hawari Y., Martin H.J., Maser E.;
RT "Bioinformatic and biochemical characterization of DCXR and DHRS2/4 from
RT Caenorhabditis elegans.";
RL Chem. Biol. Interact. 191:75-82(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21477590; DOI=10.1016/j.febslet.2011.03.062;
RA Son L.T., Ko K.M., Cho J.H., Singaravelu G., Chatterjee I., Choi T.W.,
RA Song H.O., Yu J.R., Park B.J., Lee S.K., Ahnn J.;
RT "DHS-21, a dicarbonyl/L-xylulose reductase (DCXR) ortholog, regulates
RT longevity and reproduction in Caenorhabditis elegans.";
RL FEBS Lett. 585:1310-1316(2011).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-xylulose, D-
CC xylulose, L-(+) erythrulose, D-erythrose, D-threose, L-ribulose, 1,4-
CC dibromo-2,3-butanedione and 2,3-heptanedione (PubMed:21477590). Also
CC active against isatin, 9,10-phenanthrenequinone, menadione, 2,3-
CC hexaenadione and 3,4-hexahenadione (PubMed:21300042). No activity
CC observed when tested using NADH rather than NADPH (PubMed:21300042).
CC {ECO:0000269|PubMed:21300042, ECO:0000269|PubMed:21477590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + xylitol = H(+) + L-xylulose + NADPH;
CC Xref=Rhea:RHEA:17025, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:17399, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.10;
CC Evidence={ECO:0000269|PubMed:21477590};
CC -!- ACTIVITY REGULATION: Strongly inhibited by 10% dimethyl sulfoxide.
CC {ECO:0000269|PubMed:21300042}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.65 mM for isatin (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21300042};
CC KM=0.66 mM for L-xylulose (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC KM=0.17 mM for L-(+) erythrulose (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC KM=0.27 mM for D-erythrose (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC KM=0.68 mM for D-threose (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC KM=2.58 mM for D-xylulose (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC KM=0.18 mM for L-ribulose (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC KM=8.54 mM for 1,4-dibromo-2,3-butanedione (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC KM=0.02 mM for 2,3-heptanedione (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
CC Note=The KM value for isatin is approximate as substrate saturation
CC was not reached. {ECO:0000269|PubMed:21300042};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q7Z4W1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21477590}.
CC Note=Detected on the cell membrane of spermatids.
CC {ECO:0000269|PubMed:21477590}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, gonad and spermatids (at
CC protein level). Expressed in intestine, uterine seam, gonadal sheath
CC cells, spermathecal-uterus valve and spermatids.
CC {ECO:0000269|PubMed:21477590}.
CC -!- DEVELOPMENTAL STAGE: Detected at the two-fold embryo stage. Expressed
CC in the intestine during L1 to L3, followed by expression in uterine
CC seam, gonadal sheath cells and spermathecal-uterus valve at L4.
CC {ECO:0000269|PubMed:21477590}.
CC -!- DISRUPTION PHENOTYPE: Reduced life span and impaired egg-laying
CC function resulting in the retention of eggs. Exogenous addition of
CC serotonin, which triggers vulval muscle contraction, or imipranine, a
CC serotonin uptake inhibitor, rescues the ability to lay eggs, showing
CC that the morphology of the vulva muscles and HSN neurons is normal.
CC {ECO:0000269|PubMed:21477590}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; Z75547; CAA99897.2; -; Genomic_DNA.
DR EMBL; Z75527; CAA99897.2; JOINED; Genomic_DNA.
DR PIR; T24180; T24180.
DR RefSeq; NP_506182.2; NM_073781.6.
DR AlphaFoldDB; Q21929; -.
DR SMR; Q21929; -.
DR BioGRID; 44761; 39.
DR STRING; 6239.R11D1.11; -.
DR EPD; Q21929; -.
DR PaxDb; Q21929; -.
DR PeptideAtlas; Q21929; -.
DR EnsemblMetazoa; R11D1.11.1; R11D1.11.1; WBGene00000984.
DR GeneID; 179741; -.
DR KEGG; cel:CELE_R11D1.11; -.
DR UCSC; R11D1.11; c. elegans.
DR CTD; 179741; -.
DR WormBase; R11D1.11; CE39954; WBGene00000984; dhs-21.
DR eggNOG; KOG1207; Eukaryota.
DR GeneTree; ENSGT00940000154873; -.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q21929; -.
DR OMA; EILVGWQ; -.
DR OrthoDB; 1051625at2759; -.
DR PhylomeDB; Q21929; -.
DR BRENDA; 1.1.1.10; 1045.
DR Reactome; R-CEL-5661270; Formation of xylulose-5-phosphate.
DR SABIO-RK; Q21929; -.
DR PRO; PR:Q21929; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000984; Expressed in larva and 3 other tissues.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:WormBase.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0005998; P:xylulose catabolic process; IDA:WormBase.
DR GO; GO:0005997; P:xylulose metabolic process; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Xylose metabolism.
FT CHAIN 1..251
FT /note="L-xylulose reductase"
FT /id="PRO_0000054549"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
SQ SEQUENCE 251 AA; 27219 MW; CB760AD64210E146 CRC64;
MPANYDFTDK RILVTGASQG IGKEICLSLA KAGAQVIAFA RNEANLLSLV KETTSLRYTI
IPIVGDVSAN EEVLFKLIVP HFPIHGLVNN AGIATNHAIG QITQQSIDRT FAVNVRGPIL
IAQLVARNFV DRQIKGSIVN ISSQAAIRPL DNHTVYCASK AALDMVTRCL ANELGSQNIR
VNSVNPTVVM TDMGRDNWSD PDKKKKMLDR MPIKRFAEVD EVVNAVLFLL SDNASMTTGS
TLPVDGGFSN N
