UAP2_ARATH
ID UAP2_ARATH Reviewed; 502 AA.
AC O64765; Q5PNR7; Q8L9P4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=UDP-N-acetylglucosamine diphosphorylase 2;
DE EC=2.7.7.23;
DE AltName: Full=N-acetylglucosamine-1-phosphate uridylyltransferase 2;
DE AltName: Full=UDP-N-acetylgalactosamine diphosphorylase 2;
DE EC=2.7.7.83;
DE AltName: Full=UTP--glucose-1-phosphate uridylyltransferase 2;
DE EC=2.7.7.9;
GN Name=GLCNAC1PUT2; Synonyms=ATUAP1; OrderedLocusNames=At2g35020;
GN ORFNames=F19I3.25;
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], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=20557289; DOI=10.1042/bj20100315;
RA Yang T., Echols M., Martin A., Bar-Peled M.;
RT "Identification and characterization of a strict and a promiscuous N-
RT acetylglucosamine-1-P uridylyltransferase in Arabidopsis.";
RL Biochem. J. 430:275-284(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25231969; DOI=10.1093/pcp/pcu127;
RA Chen Y.H., Shen H.L., Hsu P.J., Hwang S.G., Cheng W.H.;
RT "N-acetylglucosamine-1-P uridylyltransferase 1 and 2 are required for
RT gametogenesis and embryo development in Arabidopsis thaliana.";
RL Plant Cell Physiol. 55:1977-1993(2014).
CC -!- FUNCTION: Uridylyltransferase involved in the biosynthesis of UDP-
CC glucosamine, an essential precursor for glycoprotein and glycolipid
CC synthesis. Can use UDP-glucosamine, the 4-epimer UDP-galactosamine and
CC UDP-glucose as substrates (PubMed:20557289). Acts redundantly with
CC GLCNAC1PUT1. Required for gametogenesis and embryo development
CC (PubMed:25231969). {ECO:0000269|PubMed:20557289,
CC ECO:0000269|PubMed:25231969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000269|PubMed:20557289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-galactosamine;
CC Xref=Rhea:RHEA:34363, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:61970, ChEBI:CHEBI:67138; EC=2.7.7.83;
CC Evidence={ECO:0000269|PubMed:20557289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:58885; EC=2.7.7.9;
CC Evidence={ECO:0000269|PubMed:20557289};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20557289};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20557289};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for GlcNAc-1-P {ECO:0000269|PubMed:20557289};
CC KM=203 uM for UTP {ECO:0000269|PubMed:20557289};
CC KM=65 uM for UDP-GlcNAc {ECO:0000269|PubMed:20557289};
CC KM=808 uM for UDP-GalNAc {ECO:0000269|PubMed:20557289};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, stipules, lateral root
CC primordia, immature anthers and at the branching points of the
CC flowering shoots. {ECO:0000269|PubMed:25231969}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants glcnac1put1 and glcnac1put2 are
CC lethal. {ECO:0000269|PubMed:25231969}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 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; GU937394; ADF80195.1; -; mRNA.
DR EMBL; AC004238; AAC12841.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09050.1; -; Genomic_DNA.
DR EMBL; AF462794; AAL58890.1; -; mRNA.
DR EMBL; BT020380; AAV85735.1; -; mRNA.
DR EMBL; AY088313; AAM65852.1; -; mRNA.
DR PIR; T00483; T00483.
DR RefSeq; NP_181047.1; NM_129054.4.
DR AlphaFoldDB; O64765; -.
DR SMR; O64765; -.
DR STRING; 3702.AT2G35020.1; -.
DR PaxDb; O64765; -.
DR PRIDE; O64765; -.
DR ProteomicsDB; 228623; -.
DR EnsemblPlants; AT2G35020.1; AT2G35020.1; AT2G35020.
DR GeneID; 818066; -.
DR Gramene; AT2G35020.1; AT2G35020.1; AT2G35020.
DR KEGG; ath:AT2G35020; -.
DR Araport; AT2G35020; -.
DR TAIR; locus:2044787; AT2G35020.
DR eggNOG; KOG2388; Eukaryota.
DR HOGENOM; CLU_025603_1_1_1; -.
DR InParanoid; O64765; -.
DR OMA; KGMYRVG; -.
DR OrthoDB; 888726at2759; -.
DR PhylomeDB; O64765; -.
DR BioCyc; ARA:AT2G35020-MON; -.
DR BioCyc; MetaCyc:AT2G35020-MON; -.
DR BRENDA; 2.7.7.23; 399.
DR SABIO-RK; O64765; -.
DR UniPathway; UPA00113; UER00533.
DR PRO; PR:O64765; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64765; baseline and differential.
DR Genevisible; O64765; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052630; F:UDP-N-acetylgalactosamine diphosphorylase activity; IDA:TAIR.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:TAIR.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0009553; P:embryo sac development; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IDA:TAIR.
DR GO; GO:0019276; P:UDP-N-acetylgalactosamine metabolic process; IDA:TAIR.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IDA:TAIR.
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 Cytoplasm; Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..502
FT /note="UDP-N-acetylglucosamine diphosphorylase 2"
FT /id="PRO_0000185770"
FT MOTIF 130..133
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOTIF 332..333
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="A -> T (in Ref. 6; AAM65852)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> E (in Ref. 6; AAM65852)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="T -> A (in Ref. 6; AAM65852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 55760 MW; 72C0F2DCF15ACAD7 CRC64;
MKEPTTEIEI ETSAVATILP PPLPPTASPH QALVERLKDY GQEDVFSLWD ELSPEERDLL
LRDIENLDLP RIDRIIRCSL HSQGLPVAAI EPVPENCVST VEERTKEDRE KWWKMGLKAI
YEGKLGVVLL SGGQGTRLGS SDPKGCYNIG LPSGKSLFQI QAERILCVQR LASQAMSEAS
PTRPVTIQWY IMTSPFTHEP TQKFFKSHKY FGLEPDQVTF FQQGTLPCIS KDGKFIMETP
FSLSKAPDGN GGVYTALKSS RLLEDMASRG IKYVDCYGVD NVLVRVADPT FLGYFIDKSA
ASAAKVVRKA YPQEKVGVFV RRGKGGPLTV VEYTELDQSM ASATNQQTGR LQYCWSNVCL
HMFTLDFLNQ VANGLEKDSV YHLAEKKIPS INGDIVGLKL EQFIFDCFPY APSTALFEVL
REEEFAPVKN ANGSNYDTPE SARLLVLRLH TRWVIAAGGF LTHSVPLYAT GVEVSPLCSY
AGENLEAICR GRTFHAPCEI SL
