USP1_SOYBN
ID USP1_SOYBN Reviewed; 600 AA.
AC Q09WE7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=UDP-sugar pyrophosphorylase 1;
DE EC=2.7.7.64;
GN Name=USP1;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Lambert;
RX AGRICOLA=IND43835961; DOI=10.1111/j.1399-3054.2006.00728.x;
RA Litterer L.A., Plaisance K.L., Schnurr J.A., Storey K.K., Jung H.-J.G.,
RA Gronwald J.W., Somers D.A.;
RT "Biosynthesis of UDP-glucuronic acid in developing soybean embryos:
RT possible role of UDP-sugar pyrophosphorylase.";
RL Physiol. Plantarum 128:200-211(2006).
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. {ECO:0000269|Ref.1}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for glucuronic acid-1-phosphate {ECO:0000269|Ref.1};
CC KM=0.23 mM for glucose-1-phosphate {ECO:0000269|Ref.1};
CC KM=0.17 mM for UTP {ECO:0000269|Ref.1};
CC Vmax=5.03 nmol/min/mg enzyme for the forward reaction with glucuronic
CC acid-1-phosphate as substrate {ECO:0000269|Ref.1};
CC Vmax=4.99 nmol/min/mg enzyme for the forward reaction with glucose-1-
CC phosphate as substrate {ECO:0000269|Ref.1};
CC Note=High activity with galactose-1-phosphate, glucose-1-phosphate or
CC glucuronic acid-1-phosphate, but low or no activity with N-
CC acetylglucosamine-1-phosphate, mannose-1-phosphate or glucose-6-
CC phosphate.;
CC pH dependence:
CC Optimum pH is 7.5-9.0. {ECO:0000269|Ref.1};
CC -!- TISSUE SPECIFICITY: Expressed in root tips, young leaves, flowers and
CC developing embryos. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the USP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ267699; ABB89732.1; -; mRNA.
DR RefSeq; NP_001237434.2; NM_001250505.1.
DR AlphaFoldDB; Q09WE7; -.
DR SMR; Q09WE7; -.
DR STRING; 3847.GLYMA04G42370.1; -.
DR PRIDE; Q09WE7; -.
DR GeneID; 778158; -.
DR KEGG; gmx:778158; -.
DR eggNOG; KOG2388; Eukaryota.
DR InParanoid; Q09WE7; -.
DR OrthoDB; 888726at2759; -.
DR BRENDA; 2.7.7.44; 2483.
DR BRENDA; 2.7.7.64; 2483.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0051748; F:UTP-monosaccharide-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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 Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..600
FT /note="UDP-sugar pyrophosphorylase 1"
FT /id="PRO_0000289980"
SQ SEQUENCE 600 AA; 66126 MW; 6261863E476584B4 CRC64;
MASSLGDNFN LLSPQQQELV KMLLDNGQEH LFRDWPAPGV DDDHKNAFFD QLTRLDSSYP
GGLEAYITNA KRLLADSKAG RNPFDGFTPS VPTGETLAFG DENYIKFEEA GVLEARKAAF
VLVAGGLGER LGYSGIKLAL PAETTTRTCF VQNYIESILA LQEASSQGES QTQIPLVIMT
SDDTHGRTLE LLESNSYFGM QPTQVTLLKQ EKVACLEDND ARLALEPQNK YKIQTKPHGH
GDVHALLYSS GILKVWYEAG LKWVLFFQDT NGLLFKAIPS ALGVSAAKQY HVNSLAVPRK
AKEAIGGITR LTHSDGRSMV INVEYNQLDP LLRASGYPDG DVNCETGYSP FPGNINQLIL
ELGHYIEELS KTGGAIQEFV NPKYKDASKT SFKSSTRLEC MMQDYPKTLP PSARVGFTVM
ETWLAYAPVK NNAEDAAKVP KGNPYHSATS GEMAIYRANS IILRKAGVQV ADPVVQVFNG
QEVEVWPRIT WKPKWGLTFN RIKSKVSGNC SISLRSTLAI KGPNIFIENL SVDGALIIDA
VDDAEVNVSG SVQNNGWVLE TVDYKDASEP EVLRIRGFKF NKIEQLETKY SEPGKFHLKA