USP_ARATH
ID USP_ARATH Reviewed; 614 AA.
AC Q9C5I1; Q9LTG1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=UDP-sugar pyrophosphorylase;
DE Short=AtUSP;
DE EC=2.7.7.64;
GN Name=USP; OrderedLocusNames=At5g52560; ORFNames=F6N7.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bar-Peled L., Bar-Peled M.;
RT "Biochemical characterization of a nonspecific UDP-sugar pyrophosphorylase
RT from Arabidopsis.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16757173; DOI=10.1016/j.plaphy.2006.04.004;
RA Litterer L.A., Schnurr J.A., Plaisance K.L., Storey K.K., Gronwald J.W.,
RA Somers D.A.;
RT "Characterization and expression of Arabidopsis UDP-sugar
RT pyrophosphorylase.";
RL Plant Physiol. Biochem. 44:171-180(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16557401; DOI=10.1007/s00425-006-0240-1;
RA Schnurr J.A., Storey K.K., Jung H.-J.G., Somers D.A., Gronwald J.W.;
RT "UDP-sugar pyrophosphorylase is essential for pollen development in
RT Arabidopsis.";
RL Planta 224:520-532(2006).
RN [7]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17341835; DOI=10.1271/bbb.60605;
RA Kotake T., Hojo S., Yamaguchi D., Aohara T., Konishi T., Tsumuraya Y.;
RT "Properties and physiological functions of UDP-sugar pyrophosphorylase in
RT Arabidopsis.";
RL Biosci. Biotechnol. Biochem. 71:761-771(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23373795; DOI=10.1111/tpj.12116;
RA Geserick C., Tenhaken R.;
RT "UDP-sugar pyrophosphorylase is essential for arabinose and xylose
RT recycling, and is required during vegetative and reproductive growth in
RT Arabidopsis.";
RL Plant J. 74:239-247(2013).
CC -!- FUNCTION: Required for the synthesis of the intine, the pectocellulosic
CC inner wall of developing pollen. May function as the terminal enzyme of
CC the myo-inositol oxidation (MIO) pathway. May also play a role in the
CC salvage pathway for synthesis of nucleotide sugars (PubMed:16557401,
CC PubMed:16757173, PubMed:23373795). Can use a wide range of substrates
CC including glucose-1-phosphate, galactose-1-phosphate, xylose-1-
CC phosphate, arabinose-1-phosphate and glucuronate-1-phosphate
CC (PubMed:17341835). {ECO:0000269|PubMed:16557401,
CC ECO:0000269|PubMed:16757173, ECO:0000269|PubMed:17341835,
CC ECO:0000269|PubMed:23373795}.
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 Evidence={ECO:0000269|PubMed:17341835};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17341835};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for glucuronic acid-1-phosphate
CC {ECO:0000269|PubMed:16757173};
CC KM=0.094 mM for glucuronic acid-1-phosphate
CC {ECO:0000269|PubMed:17341835};
CC KM=0.42 mM for glucose-1-phosphate {ECO:0000269|PubMed:16757173};
CC KM=0.23 mM for glucose-1-phosphate {ECO:0000269|PubMed:17341835};
CC KM=0.27 mM for galactose-1-phosphate {ECO:0000269|PubMed:17341835};
CC KM=1.5 mM for arabinose-1-phosphate {ECO:0000269|PubMed:17341835};
CC KM=1 mM for xylose-1-phosphate {ECO:0000269|PubMed:17341835};
CC KM=0.16 mM for UTP {ECO:0000269|PubMed:16757173};
CC KM=0.56 mM for UDP-glucuronic acid {ECO:0000269|PubMed:16757173};
CC KM=0.72 mM for UPD-glucose {ECO:0000269|PubMed:16757173};
CC KM=0.28 mM for UPD-glucose {ECO:0000269|PubMed:17341835};
CC KM=0.15 mM for pyrophosphate {ECO:0000269|PubMed:16757173};
CC KM=0.16 mM for pyrophosphate {ECO:0000269|PubMed:17341835};
CC Vmax=3.47 nmol/min/mg enzyme for the forward reaction with glucuronic
CC acid-1-phosphate as substrate {ECO:0000269|PubMed:16757173};
CC Vmax=5.76 nmol/min/mg enzyme for the forward reaction with glucose-1-
CC phosphate as substrate {ECO:0000269|PubMed:16757173};
CC Vmax=4.24 nmol/min/mg enzyme for the reverse reaction with UDP-
CC glucuronic acid as substrate {ECO:0000269|PubMed:16757173};
CC Vmax=4.95 nmol/min/mg enzyme for the reverse reaction with UDP-
CC glucose as substrate {ECO:0000269|PubMed:16757173};
CC Note=High activity with glucose-1-phosphate > glucuronic acid-1-
CC phosphate > galactose-1-phosphate, but low or no activity with N-
CC acetylglucosamine-1-phosphate, fucose-1-phosphate, mannose-1-
CC phosphate, inositol-1-phosphate or glucose-6-phosphate.;
CC pH dependence:
CC Optimum pH is 7.5-8.5. Inactive at or below pH 5.0.
CC {ECO:0000269|PubMed:16757173};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:16757173};
CC -!- TISSUE SPECIFICITY: Ubiquitous, but most abundant in rosette leaves,
CC inflorescences, stems, stamens and pollen.
CC {ECO:0000269|PubMed:16757173}.
CC -!- DEVELOPMENTAL STAGE: Expressed during pollen development, peaking at
CC the tricellular stage. {ECO:0000269|PubMed:16757173}.
CC -!- DISRUPTION PHENOTYPE: Plants produce collapsed, nonviable pollen grains
CC (PubMed:16557401, PubMed:23373795). Male sterility (PubMed:17341835).
CC {ECO:0000269|PubMed:16557401, ECO:0000269|PubMed:17341835,
CC ECO:0000269|PubMed:23373795}.
CC -!- SIMILARITY: Belongs to the USP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ324529; ABC55066.1; -; mRNA.
DR EMBL; AB025606; BAA98074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96234.1; -; Genomic_DNA.
DR EMBL; AF360236; AAK25946.1; -; mRNA.
DR EMBL; AY040035; AAK64093.1; -; mRNA.
DR RefSeq; NP_568775.1; NM_124635.4.
DR AlphaFoldDB; Q9C5I1; -.
DR SMR; Q9C5I1; -.
DR STRING; 3702.AT5G52560.1; -.
DR iPTMnet; Q9C5I1; -.
DR PaxDb; Q9C5I1; -.
DR PRIDE; Q9C5I1; -.
DR ProteomicsDB; 228664; -.
DR EnsemblPlants; AT5G52560.1; AT5G52560.1; AT5G52560.
DR GeneID; 835333; -.
DR Gramene; AT5G52560.1; AT5G52560.1; AT5G52560.
DR KEGG; ath:AT5G52560; -.
DR Araport; AT5G52560; -.
DR TAIR; locus:2149574; AT5G52560.
DR eggNOG; KOG2388; Eukaryota.
DR HOGENOM; CLU_016797_0_0_1; -.
DR InParanoid; Q9C5I1; -.
DR OMA; PMGPRVV; -.
DR OrthoDB; 888726at2759; -.
DR PhylomeDB; Q9C5I1; -.
DR BioCyc; ARA:AT5G52560-MON; -.
DR BioCyc; MetaCyc:AT5G52560-MON; -.
DR BRENDA; 2.7.7.44; 399.
DR BRENDA; 2.7.7.64; 399.
DR PRO; PR:Q9C5I1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5I1; baseline and differential.
DR Genevisible; Q9C5I1; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0047350; F:glucuronate-1-phosphate uridylyltransferase activity; IDA:TAIR.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0051748; F:UTP-monosaccharide-1-phosphate uridylyltransferase activity; ISS:TAIR.
DR GO; GO:0010491; F:UTP:arabinose-1-phosphate uridylyltransferase activity; IDA:TAIR.
DR GO; GO:0017103; F:UTP:galactose-1-phosphate uridylyltransferase activity; IDA:TAIR.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IDA:TAIR.
DR GO; GO:0047338; F:UTP:xylose-1-phosphate uridylyltransferase activity; IDA:TAIR.
DR GO; GO:0009226; P:nucleotide-sugar biosynthetic process; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0052573; P:UDP-D-galactose metabolic process; IDA:TAIR.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IDA:TAIR.
DR GO; GO:0046398; P:UDP-glucuronate metabolic process; IDA:TAIR.
DR GO; GO:0033356; P:UDP-L-arabinose metabolic process; IMP:TAIR.
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 Acetylation; Nucleotidyltransferase; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..614
FT /note="UDP-sugar pyrophosphorylase"
FT /id="PRO_0000289978"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 614 AA; 67852 MW; A83D823026E1BDA8 CRC64;
MASTVDSNFF SSVPALHSNL GLLSPDQIEL AKILLENGQS HLFQQWPELG VDDKEKLAFF
DQIARLNSSY PGGLAAYIKT AKELLADSKV GKNPYDGFSP SVPSGENLTF GTDNFIEMEK
RGVVEARNAA FVLVAGGLGE RLGYNGIKVA LPRETTTGTC FLQHYIESIL ALQEASNKID
SDGSERDIPF IIMTSDDTHS RTLDLLELNS YFGMKPTQVH LLKQEKVACL DDNDARLALD
PHNKYSIQTK PHGHGDVHSL LYSSGLLHKW LEAGLKWVLF FQDTNGLLFN AIPASLGVSA
TKQYHVNSLA VPRKAKEAIG GISKLTHVDG RSMVINVEYN QLDPLLRASG FPDGDVNCET
GFSPFPGNIN QLILELGPYK DELQKTGGAI KEFVNPKYKD STKTAFKSST RLECMMQDYP
KTLPPTARVG FTVMDIWLAY APVKNNPEDA AKVPKGNPYH SATSGEMAIY RANSLILQKA
GVKVEEPVKQ VLNGQEVEVW SRITWKPKWG MIFSDIKKKV SGNCEVSQRS TMAIKGRNVF
IKDLSLDGAL IVDSIDDAEV KLGGLIKNNG WTMESVDYKD TSVPEEIRIR GFRFNKVEQL
EKKLTQPGKF SVED
