UTP--glucose-1-phosphate uridylyltransferase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P32861 (UGPA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
UTP--glucose-1-phosphate uridylyltransferase
EC=2.7.7.9

Alternative name(s):
UDP-glucose pyrophosphorylase
Short name=UDPGP
Short name=UGPase

Gene names

Name:	UGP1
Ordered Locus Names:	YKL035W
ORF Names:	YKL248

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a central role as a glucosyl donor in cellular metabolic pathways. Ref.4
Catalytic activity	UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.
Subunit structure	Homooctamer. Ref.11
Miscellaneous	Present with 17200 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the UDPGP type 1 family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	(1->6)-beta-D-glucan biosynthetic process Inferred from mutant phenotype PubMed 17531808. Source: SGD UDP-glucose metabolic process Inferred from mutant phenotype Ref.4 PubMed 9252577. Source: SGD glycogen biosynthetic process Inferred from mutant phenotype PubMed 9252577. Source: SGD trehalose biosynthetic process Inferred from genetic interaction PubMed 9252577. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity Inferred from mutant phenotype Ref.4. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSK2	Q08217	3	EBI-19987,EBI-9839

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 499

499

UTP--glucose-1-phosphate uridylyltransferase

PRO_0000185765

Regions

Region

448 – 499

Oligomerization

Sites

Active site

388

Probable

Metal binding

123

Magnesium Probable

Metal binding

246

Magnesium Probable

Amino acid modifications

Modified residue

Phosphothreonine Ref.8 Ref.9 Ref.10

Modified residue

Phosphoserine Ref.5 Ref.7 Ref.8 Ref.10

Modified residue

Phosphothreonine Ref.8 Ref.10

Modified residue

Phosphotyrosine Ref.10

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphothreonine Ref.8

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphoserine Ref.10

Modified residue

102

Phosphoserine Ref.10

Modified residue

116

Phosphoserine Ref.10

Modified residue

183

Phosphoserine Ref.9

Modified residue

391

Phosphoserine Ref.10

Secondary structure

499

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32861 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 9B9F4BED885E004D
Show »

FASTA

499

55,988

        10         20         30         40         50         60 
MSTKKHTKTH STYAFESNTN SVAASQMRNA LNKLADSSKL DDAARAKFEN ELDSFFTLFR 

        70         80         90        100        110        120 
RYLVEKSSRT TLEWDKIKSP NPDEVVKYEI ISQQPENVSN LSKLAVLKLN GGLGTSMGCV 

       130        140        150        160        170        180 
GPKSVIEVRE GNTFLDLSVR QIEYLNRQYD SDVPLLLMNS FNTDKDTEHL IKKYSANRIR 

       190        200        210        220        230        240 
IRSFNQSRFP RVYKDSLLPV PTEYDSPLDA WYPPGHGDLF ESLHVSGELD ALIAQGREIL 

       250        260        270        280        290        300 
FVSNGDNLGA TVDLKILNHM IETGAEYIME LTDKTRADVK GGTLISYDGQ VRLLEVAQVP 

       310        320        330        340        350        360 
KEHIDEFKNI RKFTNFNTNN LWINLKAVKR LIESSNLEME IIPNQKTITR DGHEINVLQL 

       370        380        390        400        410        420 
ETACGAAIRH FDGAHGVVVP RSRFLPVKTC SDLLLVKSDL FRLEHGSLKL DPSRFGPNPL 

       430        440        450        460        470        480 
IKLGSHFKKV SGFNARIPHI PKIVELDHLT ITGNVFLGKD VTLRGTVIIV CSDGHKIDIP 

       490 
NGSILENVVV TGNLQILEH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of a 12 kb fragment on the left arm of yeast chromosome XI reveals five new open reading frames, including a zinc finger protein and a homolog of the UDP-glucose pyrophosphorylase from potato." Purnelle B., Skala J., van Dyck L., Goffeau A. Yeast 8:977-986(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Genetic and biochemical characterization of the UGP1 gene encoding the UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae." Daran J.M., Dallies N., Thines-Sempoux D., Paquet V., Francois J. Eur. J. Biochem. 233:520-530(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY. Strain: 2124.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-11; THR-12; SER-17; THR-19 AND SER-21, MASS SPECTROMETRY.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-183, MASS SPECTROMETRY.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-11; THR-12; TYR-13; SER-79; SER-102; SER-116 AND SER-391, MASS SPECTROMETRY.
[11]	"Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae." Roeben A., Plitzko J.M., Korner R., Bottcher U.M., Siegers K., Hayer-Hartl M., Bracher A. J. Mol. Biol. 364:551-560(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 12-499, SUBUNIT, OLIGOMERIZATION REGION, PROBABLE MAGNESIUM-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X69584 Genomic DNA. Translation: CAA49303.1.
Z28035 Genomic DNA. Translation: CAA81872.1.
BK006944 Genomic DNA. Translation: DAA09120.1.

PIR

S30007.

RefSeq

NP_012889.3. NM_001179601.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I5K	X-ray	3.10	A/B	12-499	[»]

ProteinModelPortal

P32861.

SMR

P32861. Positions 20-499.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4534N.

IntAct

P32861. 16 interactions.

MINT

MINT-488090.

STRING

4932.YKL035W.

Proteomic databases

PaxDb

P32861.

PeptideAtlas

P32861.

PRIDE

P32861.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKL035W; YKL035W; YKL035W.

GeneID

853830.

KEGG

sce:YKL033W-A.
sce:YKL035W.

Organism-specific databases

CYGD

YKL035w.

SGD

S000001518. UGP1.

Phylogenomic databases

eggNOG

COG4284.

GeneTree

ENSGT00390000003174.

HOGENOM

HOG000113618.

K00963.

OMA

PPNGKRC.

OrthoDB

EOG4KSST8.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-17138.

Gene expression databases

Genevestigator

P32861.

GermOnline

YKL035W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002618. UDPGP_trans.
IPR016267. UDPGP_trans_subgr.
[Graphical view]

PANTHER

PTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.

Pfam

PF01704. UDPGP. 1 hit.
[Graphical view]

PIRSF

PIRSF000806. UDPGP. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P32861.

NextBio

975029.

Entry information

Entry name

UGPA1_YEAST

Accession

Primary (citable) accession number: P32861
Secondary accession number(s): D6VXQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents