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   24-JAN-2024, entry version 151.
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}.
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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.O64765; -.
DR   iPTMnet; O64765; -.
DR   PaxDb; 3702-AT2G35020-1; -.
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; AT2G35020; GLCNAC1PUT2.
DR   eggNOG; KOG2388; Eukaryota.
DR   HOGENOM; CLU_025603_1_1_1; -.
DR   InParanoid; O64765; -.
DR   OMA; WYVMTSE; -.
DR   OrthoDB; 5485456at2759; -.
DR   PhylomeDB; O64765; -.
DR   BioCyc; ARA:AT2G35020-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G35020-MONOMER; -.
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   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; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IDA:TAIR.
DR   CDD; cd04193; UDPGlcNAc_PPase; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR   InterPro; IPR002618; UDPGP_fam.
DR   PANTHER; PTHR11952:SF2; LD24639P; 1.
DR   PANTHER; PTHR11952; UDP- GLUCOSE PYROPHOSPHORYLASE; 1.
DR   Pfam; PF01704; UDPGP; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; O64765; AT.
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
//