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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
 
 
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