UAP1_ARATH
ID UAP1_ARATH Reviewed; 505 AA.
AC Q940S3; Q9FYJ8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=UDP-N-acetylglucosamine diphosphorylase 1;
DE EC=2.7.7.23;
DE AltName: Full=N-acetylglucosamine-1-phosphate uridylyltransferase 1;
DE AltName: Full=UDP-N-acetylgalactosamine diphosphorylase 1;
DE EC=2.7.7.83;
GN Name=GLCNAC1PUT1; OrderedLocusNames=At1g31070; ORFNames=F17F8.1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND 3D-STRUCTURE
RP MODELING.
RC STRAIN=cv. Columbia;
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 [5]
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 both UDP-glucosamine and the 4-epimer UDP-
CC galactosamine as substrates, but no other sugars or NTPs
CC (PubMed:20557289). Acts redundantly with GLCNAC1PUT2. Required for
CC gametogenesis and embryo development (PubMed:25231969).
CC {ECO:0000269|PubMed:20557289, 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 -!- 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 -!- ACTIVITY REGULATION: Inhibited by hygromycin and streptomycin, but not
CC by gentamycin or kanamycin. {ECO:0000269|PubMed:20557289}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=337 uM for GlcNAc-1-P {ECO:0000269|PubMed:20557289};
CC KM=295 uM for UTP {ECO:0000269|PubMed:20557289};
CC KM=219 uM for UDP-GlcNAc {ECO:0000269|PubMed:20557289};
CC KM=2768 uM for UDP-GalNAc {ECO:0000269|PubMed:20557289};
CC pH dependence:
CC Optimum pH is 7.6-8.0. {ECO:0000269|PubMed:20557289};
CC Temperature dependence:
CC Optimum temperature is 30-37 degrees Celsius.
CC {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:0000269|PubMed:20557289}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q940S3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in root tips, stipules and mature pollen
CC grains. {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 -!- SEQUENCE CAUTION:
CC Sequence=AAF98204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF98204.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC000107; AAF98204.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31311.1; -; Genomic_DNA.
DR EMBL; AY053411; AAK96641.1; -; mRNA.
DR PIR; B86436; B86436.
DR RefSeq; NP_564372.3; NM_102845.5. [Q940S3-1]
DR AlphaFoldDB; Q940S3; -.
DR SMR; Q940S3; -.
DR STRING; 3702.AT1G31070.2; -.
DR iPTMnet; Q940S3; -.
DR PaxDb; Q940S3; -.
DR PRIDE; Q940S3; -.
DR ProteomicsDB; 228710; -. [Q940S3-1]
DR EnsemblPlants; AT1G31070.2; AT1G31070.2; AT1G31070. [Q940S3-1]
DR GeneID; 839993; -.
DR Gramene; AT1G31070.2; AT1G31070.2; AT1G31070. [Q940S3-1]
DR KEGG; ath:AT1G31070; -.
DR Araport; AT1G31070; -.
DR TAIR; locus:2015791; AT1G31070.
DR eggNOG; KOG2388; Eukaryota.
DR HOGENOM; CLU_025603_1_1_1; -.
DR InParanoid; Q940S3; -.
DR OMA; QPDVLKF; -.
DR PhylomeDB; Q940S3; -.
DR BioCyc; ARA:AT1G31070-MON; -.
DR BRENDA; 2.7.7.23; 399.
DR SABIO-RK; Q940S3; -.
DR UniPathway; UPA00113; UER00533.
DR PRO; PR:Q940S3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q940S3; baseline and differential.
DR Genevisible; Q940S3; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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: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: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 Alternative splicing; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..505
FT /note="UDP-N-acetylglucosamine diphosphorylase 1"
FT /id="PRO_0000421832"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..137
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOTIF 335..336
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 11..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 55992 MW; CA139F5AEB45003E CRC64;
MIEPSMEREN GALTAATTTT TAVTSPPPMA SSPRQALVER LKDYGQEDIF SLWDELSPDE
KDFLVRDIEN LDLPRIDRII RCSLHSQGLP VAAIEPVPEN WVSTVDGRTM EDREKWWKMG
LKTIYEGKLG VVLLSGGQGT RLGSSDPKGC FNIGLPSGKS LFQIQAERIL CVQRLAAQVV
SEGPIRPVTI HWYIMTSPFT DEATRKYFSS HKYFGLEPDQ ISFFQQGTLP CVTKDGKFIM
ETPFSLAKAP DGNGGVYAAL KCSRLLEDMA SRGIKYVDCY GVDNVLVRVA DPTFLGYFID
KGAASAAKVV RKAYPQEQVG VFVRRGKGGP LTVVEYSELD QSMASAINQR TGRLQYCWSN
VCLHMFTLDF LNQVATGLEK DSVYHLAEKK IPSMNGYTMG LKLEQFIFDS FPYAPSTALF
EVLREEEFAP VKNVNGSNFD TPESARLLVL RLHTRWVIAA GGFLTHSVPL YATGVEVSPL
CSYAGENLEA ICRGRTFHAP CEISL
