Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable UTP--glucose-1-phosphate uridylyltransferase 2

Gene

At3g03250

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role as a glucosyl donor in cellular metabolic pathways.By similarity

Catalytic activityi

UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.

GO - Molecular functioni

GO - Biological processi

  • callose deposition in cell wall Source: TAIR
  • cellular response to phosphate starvation Source: TAIR
  • pollen development Source: TAIR
  • response to salt stress Source: TAIR
  • sucrose metabolic process Source: TAIR
  • UDP-glucose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Enzyme and pathway databases

BioCyciARA:AT3G03250-MONOMER.
MetaCyc:AT3G03250-MONOMER.
BRENDAi2.7.7.9. 399.
ReactomeiREACT_310241. Formation of the active cofactor, UDP-glucuronate.
REACT_353817. Glycogen synthesis.
SABIO-RKQ9M9P3.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable UTP--glucose-1-phosphate uridylyltransferase 2 (EC:2.7.7.9)
Alternative name(s):
UDP-glucose pyrophosphorylase 2
Short name:
UDPGP 2
Short name:
UGPase 2
Gene namesi
Ordered Locus Names:At3g03250
ORF Names:T17B22.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G03250.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
  • pollen tube Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 469468Probable UTP--glucose-1-phosphate uridylyltransferase 2PRO_0000185757Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9M9P3.
PRIDEiQ9M9P3.

Interactioni

Protein-protein interaction databases

BioGridi6646. 1 interaction.
STRINGi3702.AT3G03250.1.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1710Combined sources
Beta strandi19 – 213Combined sources
Helixi23 – 3614Combined sources
Helixi46 – 483Combined sources
Turni54 – 563Combined sources
Beta strandi57 – 593Combined sources
Helixi60 – 623Combined sources
Helixi70 – 778Combined sources
Beta strandi80 – 867Combined sources
Helixi91 – 933Combined sources
Beta strandi96 – 983Combined sources
Helixi99 – 1013Combined sources
Beta strandi102 – 1054Combined sources
Helixi110 – 12516Combined sources
Beta strandi131 – 1355Combined sources
Turni137 – 1393Combined sources
Helixi140 – 1478Combined sources
Helixi148 – 1503Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi157 – 1615Combined sources
Turni170 – 1734Combined sources
Helixi176 – 1794Combined sources
Helixi184 – 1863Combined sources
Helixi192 – 1943Combined sources
Helixi195 – 2028Combined sources
Helixi204 – 2096Combined sources
Beta strandi215 – 2206Combined sources
Helixi230 – 23910Combined sources
Beta strandi242 – 2498Combined sources
Helixi252 – 2543Combined sources
Beta strandi259 – 2635Combined sources
Beta strandi266 – 2705Combined sources
Helixi272 – 2743Combined sources
Helixi277 – 2793Combined sources
Helixi280 – 2845Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi291 – 30010Combined sources
Helixi301 – 3099Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi327 – 3304Combined sources
Helixi336 – 3427Combined sources
Beta strandi347 – 3504Combined sources
Helixi353 – 3553Combined sources
Helixi362 – 3698Combined sources
Beta strandi373 – 3764Combined sources
Beta strandi379 – 3824Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi393 – 3964Combined sources
Helixi398 – 4003Combined sources
Helixi403 – 4086Combined sources
Beta strandi410 – 4123Combined sources
Beta strandi419 – 43012Combined sources
Beta strandi435 – 4439Combined sources
Beta strandi449 – 4524Combined sources
Beta strandi457 – 4604Combined sources
Helixi466 – 4683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z90X-ray1.86A/B1-469[»]
2ICXX-ray1.85A/B2-469[»]
2ICYX-ray1.64A/B2-469[»]
2Q4JX-ray1.86A/B1-469[»]
ProteinModelPortaliQ9M9P3.
SMRiQ9M9P3. Positions 7-469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9M9P3.

Family & Domainsi

Sequence similaritiesi

Belongs to the UDPGP type 1 family.Curated

Phylogenomic databases

eggNOGiCOG4284.
HOGENOMiHOG000113618.
InParanoidiQ9M9P3.
KOiK00963.
OMAiSERANAQ.
PhylomeDBiQ9M9P3.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR016267. UDPGP_trans.
IPR002618. UDPGP_trans_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFiPIRSF000806. UDPGP. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9M9P3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATTENLPQ LKSAVDGLTE MSESEKSGFI SLVSRYLSGE AQHIEWSKIQ
60 70 80 90 100
TPTDEIVVPY EKMTPVSQDV AETKNLLDKL VVLKLNGGLG TTMGCTGPKS
110 120 130 140 150
VIEVRDGLTF LDLIVIQIEN LNNKYGCKVP LVLMNSFNTH DDTHKIVEKY
160 170 180 190 200
TNSNVDIHTF NQSKYPRVVA DEFVPWPSKG KTDKEGWYPP GHGDVFPALM
210 220 230 240 250
NSGKLDTFLS QGKEYVFVAN SDNLGAIVDL TILKHLIQNK NEYCMEVTPK
260 270 280 290 300
TLADVKGGTL ISYEGKVQLL EIAQVPDEHV NEFKSIEKFK IFNTNNLWVN
310 320 330 340 350
LKAIKKLVEA DALKMEIIPN PKEVDGVKVL QLETAAGAAI RFFDNAIGVN
360 370 380 390 400
VPRSRFLPVK ASSDLLLVQS DLYTLVDGFV TRNKARTNPS NPSIELGPEF
410 420 430 440 450
KKVATFLSRF KSIPSIVELD SLKVSGDVWF GSSIVLKGKV TVAAKSGVKL
460
EIPDRAVVEN KNINGPEDL
Length:469
Mass (Da):51,738
Last modified:October 1, 2000 - v1
Checksum:iD0B70B92A2372820
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871W → R in AAK32773 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012328 Genomic DNA. Translation: AAF26102.1.
CP002686 Genomic DNA. Translation: AEE73917.1.
AY035071 mRNA. Translation: AAK59576.1.
AY059148 mRNA. Translation: AAL15254.1.
AF361605 mRNA. Translation: AAK32773.1.
RefSeqiNP_186975.1. NM_111195.3.
UniGeneiAt.24250.

Genome annotation databases

EnsemblPlantsiAT3G03250.1; AT3G03250.1; AT3G03250.
GeneIDi821313.
KEGGiath:AT3G03250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012328 Genomic DNA. Translation: AAF26102.1.
CP002686 Genomic DNA. Translation: AEE73917.1.
AY035071 mRNA. Translation: AAK59576.1.
AY059148 mRNA. Translation: AAL15254.1.
AF361605 mRNA. Translation: AAK32773.1.
RefSeqiNP_186975.1. NM_111195.3.
UniGeneiAt.24250.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z90X-ray1.86A/B1-469[»]
2ICXX-ray1.85A/B2-469[»]
2ICYX-ray1.64A/B2-469[»]
2Q4JX-ray1.86A/B1-469[»]
ProteinModelPortaliQ9M9P3.
SMRiQ9M9P3. Positions 7-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi6646. 1 interaction.
STRINGi3702.AT3G03250.1.

Proteomic databases

PaxDbiQ9M9P3.
PRIDEiQ9M9P3.

Protocols and materials databases

DNASUi821313.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G03250.1; AT3G03250.1; AT3G03250.
GeneIDi821313.
KEGGiath:AT3G03250.

Organism-specific databases

TAIRiAT3G03250.

Phylogenomic databases

eggNOGiCOG4284.
HOGENOMiHOG000113618.
InParanoidiQ9M9P3.
KOiK00963.
OMAiSERANAQ.
PhylomeDBiQ9M9P3.

Enzyme and pathway databases

BioCyciARA:AT3G03250-MONOMER.
MetaCyc:AT3G03250-MONOMER.
BRENDAi2.7.7.9. 399.
ReactomeiREACT_310241. Formation of the active cofactor, UDP-glucuronate.
REACT_353817. Glycogen synthesis.
SABIO-RKQ9M9P3.

Miscellaneous databases

EvolutionaryTraceiQ9M9P3.
PROiQ9M9P3.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR016267. UDPGP_trans.
IPR002618. UDPGP_trans_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFiPIRSF000806. UDPGP. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  5. "X-ray structure of gene product from Arabidopsis thaliana At3g03250, a putative UDP-glucose pyrophosphorylase."
    Center for eukaryotic structural genomics (CESG)
    Submitted (APR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 1-469.

Entry informationi

Entry nameiUGPA2_ARATH
AccessioniPrimary (citable) accession number: Q9M9P3
Secondary accession number(s): Q9ASY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.