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USP_PEA
ID   USP_PEA                 Reviewed;         600 AA.
AC   Q5W915;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=UDP-sugar pyrophospharylase;
DE            Short=PsUSP;
DE            EC=2.7.7.64;
GN   Name=USP;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 325-339, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15326166; DOI=10.1074/jbc.m408716200;
RA   Kotake T., Yamaguchi D., Ohzono H., Hojo S., Kaneko S., Ishida H.,
RA   Tsumuraya Y.;
RT   "UDP-sugar pyrophosphorylase with broad substrate specificity toward
RT   various monosaccharide 1-phosphates from pea sprouts.";
RL   J. Biol. Chem. 279:45728-45736(2004).
CC   -!- FUNCTION: May function as the terminal enzyme of the myo-inositol
CC       oxidation (MIO) pathway. May also play a role in the salvage pathway
CC       for synthesis of nucleotide sugars.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monosaccharide 1-phosphate + H(+) + UTP = a UDP-
CC         monosaccharide + diphosphate; Xref=Rhea:RHEA:13205,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:140358, ChEBI:CHEBI:140359; EC=2.7.7.64;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- ACTIVITY REGULATION: Inhibited by a high concentration of
CC       pyrophosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.048 mM for UTP {ECO:0000269|PubMed:15326166};
CC         KM=0.34 mM for glucose-1-phosphate {ECO:0000269|PubMed:15326166};
CC         KM=0.58 mM for galactose-1-phosphate {ECO:0000269|PubMed:15326166};
CC         KM=0.48 mM for glucuronic acid-1-phosphate
CC         {ECO:0000269|PubMed:15326166};
CC         KM=0.96 mM for arabinose-1-phosphate {ECO:0000269|PubMed:15326166};
CC         KM=1.98 mM for xylose-1-phosphate {ECO:0000269|PubMed:15326166};
CC         KM=0.34 mM for UPD-glucose {ECO:0000269|PubMed:15326166};
CC         KM=0.25 mM for pyrophosphate {ECO:0000269|PubMed:15326166};
CC         Vmax=81 umol/min/mg enzyme for the forward reaction with UTP as
CC         substrate {ECO:0000269|PubMed:15326166};
CC         Vmax=106 umol/min/mg enzyme for the forward reaction with glucose-1-
CC         phosphate as substrate {ECO:0000269|PubMed:15326166};
CC         Vmax=161 umol/min/mg enzyme for the forward reaction with galactose-
CC         1-phosphate as substrate {ECO:0000269|PubMed:15326166};
CC         Vmax=66 umol/min/mg enzyme for the forward reaction with glucuronic
CC         acid-1-phosphate as substrate {ECO:0000269|PubMed:15326166};
CC         Vmax=71 umol/min/mg enzyme for the forward reaction with arabinose-1-
CC         phosphate as substrate {ECO:0000269|PubMed:15326166};
CC         Vmax=49 umol/min/mg enzyme for the forward reaction with xylose-1-
CC         phosphate as substrate {ECO:0000269|PubMed:15326166};
CC         Vmax=145 umol/min/mg enzyme for the reverse reaction with UDP-glucose
CC         as substrate {ECO:0000269|PubMed:15326166};
CC         Vmax=64 umol/min/mg enzyme for the reverse reaction with
CC         pyrophosphate as substrate {ECO:0000269|PubMed:15326166};
CC         Note=High activity with galactose-1-phosphate > glucose-1-phosphate >
CC         glucuronic acid-1-phosphate, but low or no activity with N-
CC         acetylglucosamine-1-phosphate, fucose-1-phosphate, mannose-1-
CC         phosphate or glucose-6-phosphate.;
CC       pH dependence:
CC         Optimum pH is 6.5-7.5. Inactive at or below pH 5.0.
CC         {ECO:0000269|PubMed:15326166};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:15326166};
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the USP family. {ECO:0000305}.
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DR   EMBL; AB178642; BAD66876.1; -; mRNA.
DR   AlphaFoldDB; Q5W915; -.
DR   SMR; Q5W915; -.
DR   KEGG; ag:BAD66876; -.
DR   BioCyc; MetaCyc:MON-11146; -.
DR   BRENDA; 2.7.7.64; 4872.
DR   SABIO-RK; Q5W915; -.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR   GO; GO:0090406; C:pollen tube; IEA:EnsemblPlants.
DR   GO; GO:0047350; F:glucuronate-1-phosphate uridylyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0010491; F:UTP:arabinose-1-phosphate uridylyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0017103; F:UTP:galactose-1-phosphate uridylyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0047338; F:UTP:xylose-1-phosphate uridylyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0009226; P:nucleotide-sugar biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0009555; P:pollen development; IEA:EnsemblPlants.
DR   GO; GO:0052573; P:UDP-D-galactose metabolic process; IEA:EnsemblPlants.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:EnsemblPlants.
DR   GO; GO:0046398; P:UDP-glucuronate metabolic process; IEA:EnsemblPlants.
DR   GO; GO:0033356; P:UDP-L-arabinose metabolic process; IEA:EnsemblPlants.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR   InterPro; IPR002618; UDPGP_fam.
DR   PANTHER; PTHR11952; PTHR11952; 1.
DR   Pfam; PF01704; UDPGP; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..600
FT                   /note="UDP-sugar pyrophospharylase"
FT                   /id="PRO_0000289983"
SQ   SEQUENCE   600 AA;  66177 MW;  F991DD8CC80786CA CRC64;
     MASSLGDNFN LLSPQQRELV KMLLDNGQDH LFRDWPNPGV DDDEKKAFFD QLVLLDSSYP
     GGLVAYINNA KRLLADSKAG NNPFDGFTPS VPTGETLKFG DENFNKYEEA GVREARRAAF
     VLVAGGLGER LGYNGIKVAL PAETTTGTCF LQHYIESILA LQEASSEGEG QTHIPFVIMT
     SDDTHGRTLD LLESNSYFGM QPTQVTLLKQ EKVACLEDND ARLALDPQNR YRVQTKPHGH
     GDVHSLLHSS GILKVWYNAG LKWVLFFQDT NGLLFKAIPS ALGVSSTKQY HVNSLAVPRK
     AKEAIGGITR LTHSDGRSMV INVEYNQLDP LLRASGYPDG DVNSETGYSP FPGNINQLIL
     ELGPYIEELA KTGGAIQEFV NPKYKDASKT SFKSSTRLEC MMQDYPKTLP PSSRVGFTVM
     ETWFAYAPVK NNAEDAAKVP KGNPYHSATS GEMAIYRANS LILKKAGFQV ADPVLQVING
     QEVEVWPRIT WKPKWGLTFS LVKSKVSGNC SISQRSTLAI KGRKIFIENL SVDGALIVDA
     VDDAEVNVSG SVQNNGWALE PVDYKDSSEP EVLRIRGFKF NKVEQVEKKY SEPGKFDFKA
 
 
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