UGPA2_ARATH
ID UGPA2_ARATH Reviewed; 469 AA.
AC Q9M9P3; Q9ASY1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase 2;
DE EC=2.7.7.9;
DE AltName: Full=UDP-glucose pyrophosphorylase 2;
DE Short=AtUGP2 {ECO:0000303|PubMed:20435647};
DE Short=UDPGP 2;
DE Short=UGPase 2;
GN Name=UGP2 {ECO:0000303|PubMed:19366709}; OrderedLocusNames=At3g03250;
GN ORFNames=T17B22.6;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY SUCROSE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19366709; DOI=10.1093/pcp/pcp052;
RA Meng M., Geisler M., Johansson H., Harholt J., Scheller H.V.,
RA Mellerowicz E.J., Kleczkowski L.A.;
RT "UDP-glucose pyrophosphorylase is not rate limiting, but is essential in
RT Arabidopsis.";
RL Plant Cell Physiol. 50:998-1011(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20435647; DOI=10.1093/pcp/pcq057;
RA Park J.I., Ishimizu T., Suwabe K., Sudo K., Masuko H., Hakozaki H.,
RA Nou I.S., Suzuki G., Watanabe M.;
RT "UDP-glucose pyrophosphorylase is rate limiting in vegetative and
RT reproductive phases in Arabidopsis thaliana.";
RL Plant Cell Physiol. 51:981-996(2010).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 2-469 IN COMPLEX WITH UTP.
RX PubMed=17178129; DOI=10.1016/j.jmb.2006.11.059;
RA McCoy J.G., Bitto E., Bingman C.A., Wesenberg G.E., Bannen R.M.,
RA Kondrashov D.A., Phillips G.N. Jr.;
RT "Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis
RT thaliana with bound UDP-glucose and UTP.";
RL J. Mol. Biol. 366:830-841(2007).
CC -!- FUNCTION: Converts glucose 1-phosphate to UDP-glucose, which is the
CC major glycosyl donor for polysaccharides. Acts redundantly with UGP1
CC and is essential for the synthesis of sucrose, starch and cell wall,
CC and callose deposition. {ECO:0000269|PubMed:19366709,
CC ECO:0000269|PubMed:20435647}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cauline leaves, flowers and siliques.
CC {ECO:0000269|PubMed:19366709}.
CC -!- INDUCTION: By sucrose. {ECO:0000269|PubMed:19366709}.
CC -!- DISRUPTION PHENOTYPE: Reduced number of seeds (PubMed:19366709). The
CC double mutants upg1 and ugp2 display severe growth defects and male
CC sterility due to the absence of callose deposition around microspores
CC (PubMed:20435647). {ECO:0000269|PubMed:19366709,
CC ECO:0000269|PubMed:20435647}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; AC012328; AAF26102.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73917.1; -; Genomic_DNA.
DR EMBL; AY035071; AAK59576.1; -; mRNA.
DR EMBL; AY059148; AAL15254.1; -; mRNA.
DR EMBL; AF361605; AAK32773.1; -; mRNA.
DR RefSeq; NP_186975.1; NM_111195.4.
DR PDB; 1Z90; X-ray; 1.86 A; A/B=1-469.
DR PDB; 2ICX; X-ray; 1.85 A; A/B=2-469.
DR PDB; 2ICY; X-ray; 1.64 A; A/B=2-469.
DR PDB; 2Q4J; X-ray; 1.86 A; A/B=1-469.
DR PDBsum; 1Z90; -.
DR PDBsum; 2ICX; -.
DR PDBsum; 2ICY; -.
DR PDBsum; 2Q4J; -.
DR AlphaFoldDB; Q9M9P3; -.
DR SMR; Q9M9P3; -.
DR BioGRID; 6646; 18.
DR STRING; 3702.AT3G03250.1; -.
DR iPTMnet; Q9M9P3; -.
DR MetOSite; Q9M9P3; -.
DR PaxDb; Q9M9P3; -.
DR PRIDE; Q9M9P3; -.
DR ProteomicsDB; 245266; -.
DR DNASU; 821313; -.
DR EnsemblPlants; AT3G03250.1; AT3G03250.1; AT3G03250.
DR GeneID; 821313; -.
DR Gramene; AT3G03250.1; AT3G03250.1; AT3G03250.
DR KEGG; ath:AT3G03250; -.
DR Araport; AT3G03250; -.
DR TAIR; locus:2097785; AT3G03250.
DR eggNOG; KOG2638; Eukaryota.
DR HOGENOM; CLU_023632_3_0_1; -.
DR InParanoid; Q9M9P3; -.
DR OMA; TNNLWAK; -.
DR PhylomeDB; Q9M9P3; -.
DR BioCyc; ARA:AT3G03250-MON; -.
DR BioCyc; MetaCyc:AT3G03250-MON; -.
DR BRENDA; 2.7.7.9; 399.
DR SABIO-RK; Q9M9P3; -.
DR EvolutionaryTrace; Q9M9P3; -.
DR PRO; PR:Q9M9P3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9P3; baseline and differential.
DR Genevisible; Q9M9P3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IBA:GO_Central.
DR GO; GO:0052543; P:callose deposition in cell wall; IGI:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; TAS:TAIR.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central.
DR CDD; cd00897; UGPase_euk; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR002618; UDPGP_fam.
DR InterPro; IPR016267; UDPGP_trans.
DR PANTHER; PTHR43511; PTHR43511; 1.
DR Pfam; PF01704; UDPGP; 1.
DR PIRSF; PIRSF000806; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..469
FT /note="UTP--glucose-1-phosphate uridylyltransferase 2"
FT /id="PRO_0000185757"
FT BINDING 85..88
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:17178129,
FT ECO:0007744|PDB:2ICX"
FT BINDING 87..88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 99
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:17178129,
FT ECO:0007744|PDB:2ICX"
FT BINDING 162
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:17178129,
FT ECO:0007744|PDB:2ICX"
FT BINDING 191
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:17178129,
FT ECO:0007744|PDB:2ICX"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 220..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 222
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:17178129,
FT ECO:0007744|PDB:2ICX"
FT BINDING 360
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:17178129,
FT ECO:0007744|PDB:2ICX"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 187
FT /note="W -> R (in Ref. 3; AAK32773)"
FT /evidence="ECO:0000305"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2Q4J"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2ICY"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2ICX"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2ICY"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:2ICY"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1Z90"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 419..430
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 435..443
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:2ICY"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:2ICY"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:2ICX"
SQ SEQUENCE 469 AA; 51738 MW; D0B70B92A2372820 CRC64;
MAATTENLPQ LKSAVDGLTE MSESEKSGFI SLVSRYLSGE AQHIEWSKIQ TPTDEIVVPY
EKMTPVSQDV AETKNLLDKL VVLKLNGGLG TTMGCTGPKS VIEVRDGLTF LDLIVIQIEN
LNNKYGCKVP LVLMNSFNTH DDTHKIVEKY TNSNVDIHTF NQSKYPRVVA DEFVPWPSKG
KTDKEGWYPP GHGDVFPALM NSGKLDTFLS QGKEYVFVAN SDNLGAIVDL TILKHLIQNK
NEYCMEVTPK TLADVKGGTL ISYEGKVQLL EIAQVPDEHV NEFKSIEKFK IFNTNNLWVN
LKAIKKLVEA DALKMEIIPN PKEVDGVKVL QLETAAGAAI RFFDNAIGVN VPRSRFLPVK
ASSDLLLVQS DLYTLVDGFV TRNKARTNPS NPSIELGPEF KKVATFLSRF KSIPSIVELD
SLKVSGDVWF GSSIVLKGKV TVAAKSGVKL EIPDRAVVEN KNINGPEDL
