UGE1_PEA
ID UGE1_PEA Reviewed; 350 AA.
AC B0M3E8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1 {ECO:0000303|PubMed:19754426};
DE EC=5.1.3.2 {ECO:0000269|PubMed:19754426};
DE EC=5.1.3.5 {ECO:0000269|PubMed:19754426};
DE AltName: Full=UDP-D-xylose 4-epimerase {ECO:0000305};
DE AltName: Full=UDP-L-arabinose 4-epimerase {ECO:0000305};
DE AltName: Full=UDP-galactose 4-epimerase 1 {ECO:0000303|PubMed:19754426};
DE AltName: Full=UDP-glucose 4-epimerase 1 {ECO:0000303|PubMed:19754426};
DE Short=PsUGE1 {ECO:0000303|PubMed:19754426};
GN Name=UGE1 {ECO:0000303|PubMed:19754426};
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 2-30, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=19754426; DOI=10.1042/bj20091025;
RA Kotake T., Takata R., Verma R., Takaba M., Yamaguchi D., Orita T.,
RA Kaneko S., Matsuoka K., Koyama T., Reiter W.D., Tsumuraya Y.;
RT "Bifunctional cytosolic UDP-glucose 4-epimerases catalyse the
RT interconversion between UDP-D-xylose and UDP-L-arabinose in plants.";
RL Biochem. J. 424:169-177(2009).
CC -!- FUNCTION: Catalyzes the interconversion between UDP-glucose and UDP-
CC galactose and the interconversion between UDP-arabinose and UDP-xylose.
CC {ECO:0000269|PubMed:19754426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2; Evidence={ECO:0000269|PubMed:19754426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-beta-L-arabinopyranose = UDP-alpha-D-xylose;
CC Xref=Rhea:RHEA:11320, ChEBI:CHEBI:57632, ChEBI:CHEBI:61457;
CC EC=5.1.3.5; Evidence={ECO:0000269|PubMed:19754426};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- ACTIVITY REGULATION: Inhibited by Hg(2+).
CC {ECO:0000269|PubMed:19754426}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.29 mM for UDP-galactose {ECO:0000269|PubMed:19754426};
CC KM=0.31 mM for UDP-glucose {ECO:0000269|PubMed:19754426};
CC KM=0.15 mM for UDP-xylose {ECO:0000269|PubMed:19754426};
CC KM=0.16 mM for UDP-arabinose {ECO:0000269|PubMed:19754426};
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:19754426};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:19754426};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000305}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose biosynthesis;
CC UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AB381885; BAG09236.2; -; mRNA.
DR AlphaFoldDB; B0M3E8; -.
DR SMR; B0M3E8; -.
DR EnsemblPlants; Psat7g036120.1; Psat7g036120.1.cds; Psat7g036120.
DR Gramene; Psat7g036120.1; Psat7g036120.1.cds; Psat7g036120.
DR BRENDA; 5.1.3.2; 4872.
DR BRENDA; 5.1.3.5; 4872.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00797; UER00772.
DR UniPathway; UPA00963; -.
DR GO; GO:0050373; F:UDP-arabinose 4-epimerase activity; IDA:UniProtKB.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033358; P:UDP-L-arabinose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Galactose metabolism; Isomerase; NAD.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19754426"
FT CHAIN 2..350
FT /note="Bifunctional UDP-glucose 4-epimerase and UDP-xylose
FT 4-epimerase 1"
FT /id="PRO_0000422187"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 15..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 36..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 67..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
SQ SEQUENCE 350 AA; 38960 MW; FE583CD7CEB39D62 CRC64;
MVASSQKILV TGGAGFIGTH TVVQLLNNGF NVSIIDNFDN SVMEAVERVR EVVGSNLSQN
LEFTLGDLRN KDDLEKLFSK SKFDAVIHFA GLKAVGESVE NPRRYFDNNL VGTINLYEVM
AKHNCKKMVF SSSATVYGQP EKIPCVEDFK LQAMNPYGRT KLFLEEIARD IQKAEPEWRI
VLLRYFNPVG AHESGKLGED PRGIPNNLMP YIQQVAVGRL PELNVYGHDY PTRDGSAIRD
YIHVMDLADG HIAALRKLFT SENIGCTAYN LGTGRGSSVL EMVAAFEKAS GKKIALKLCP
RRPGDATEVY ASTAKAEKEL GWKAKYGVEE MCRDQWNWAK NNPWGYSGKP
