DER_CHICK
ID DER_CHICK Reviewed; 246 AA.
AC Q8JIS3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=D-erythrulose reductase;
DE EC=1.1.1.162;
DE AltName: Full=Probable L-xylulose reductase;
DE Short=XR;
DE EC=1.1.1.10;
GN Name=DER;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-56; 175-193 AND 211-225,
RP TISSUE SPECIFICITY, AND BLOCKAGE OF N-TERMINUS.
RC TISSUE=Liver;
RX PubMed=12200544; DOI=10.1093/protein/15.7.611;
RA Maeda M., Kaku H., Shimada M., Nishioka T.;
RT "Cloning and sequence analysis of D-erythrulose reductase from chicken: its
RT close structural relation to tetrameric carbonyl reductases.";
RL Protein Eng. 15:611-617(2002).
RN [2]
RP CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=7358641; DOI=10.1093/oxfordjournals.jbchem.a132751;
RA Uehara K., Mannen S., Hosomi S., Miyashita T.;
RT "Studies on D-tetrose metabolism. Crystallization and properties of D-
RT erythrulose reductase from chicken liver.";
RL J. Biochem. 87:47-55(1980).
CC -!- FUNCTION: Catalyzes the reduction of D-erythrulose to D-threitol with
CC the concomitant oxidation of NAD(P)H to NAD(P)(+). NADH is less
CC effective than NADPH. May also catalyze the reduction of L-xylulose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threitol + NADP(+) = D-erythrulose + H(+) + NADPH;
CC Xref=Rhea:RHEA:18005, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023,
CC ChEBI:CHEBI:48300, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.162;
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for D-erythrulose {ECO:0000269|PubMed:7358641};
CC KM=67 uM for NADH {ECO:0000269|PubMed:7358641};
CC KM=7.9 uM for NADPH {ECO:0000269|PubMed:7358641};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7358641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, and also found in high
CC amounts in liver and testis. Low expression seen in all other tissues
CC tested. {ECO:0000269|PubMed:12200544}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB049356; BAB97210.1; -; mRNA.
DR RefSeq; NP_989556.1; NM_204225.1.
DR AlphaFoldDB; Q8JIS3; -.
DR SMR; Q8JIS3; -.
DR STRING; 9031.ENSGALP00000004484; -.
DR PaxDb; Q8JIS3; -.
DR Ensembl; ENSGALT00000004493; ENSGALP00000004484; ENSGALG00000002849.
DR GeneID; 374066; -.
DR KEGG; gga:374066; -.
DR CTD; 51181; -.
DR VEuPathDB; HostDB:geneid_374066; -.
DR eggNOG; KOG1207; Eukaryota.
DR GeneTree; ENSGT00940000154873; -.
DR InParanoid; Q8JIS3; -.
DR OMA; GICEFKE; -.
DR OrthoDB; 1051625at2759; -.
DR PhylomeDB; Q8JIS3; -.
DR SABIO-RK; Q8JIS3; -.
DR PRO; PR:Q8JIS3; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000002849; Expressed in kidney and 13 other tissues.
DR ExpressionAtlas; Q8JIS3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0047880; F:erythrulose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0005997; P:xylulose metabolic process; IBA:GO_Central.
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; Cytoplasm; Direct protein sequencing; NADP;
KW Oxidoreductase; Reference proteome; Xylose metabolism.
FT CHAIN 1..246
FT /note="D-erythrulose reductase"
FT /id="PRO_0000054566"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 246 AA; 26167 MW; EAA7C3D95ACCE64F CRC64;
MEPDLSFRGR RALVTGAGKG IGRAVAVALC KAGARVTALS RTAADLESLV RECPGIEPLC
LDLADWDATE AAVGAAGPFE LLVNNAAVAM LQPFLQVTRE AVERSFDVNF RAVLHVSQIV
ARQMIAQGLP GAIVNVSSQA SQRALRDHAV YCSTKSALDM LSKVMAMELG PHKIRVNTVN
PTVVMTDMGR INWSDPQKSA AMINRIPLGK FAEVDDVVNS ILFLLSDKSA MTTGSSLMVD
GGFLVS