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P32861 (UGPA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PSK2Q082173EBI-19987,EBI-9839

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 499498UTP--glucose-1-phosphate uridylyltransferase
PRO_0000185765

Regions

Region448 – 49952Oligomerization

Sites

Active site3881 Probable
Metal binding1231Magnesium Probable
Metal binding2461Magnesium Probable

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue171Phosphoserine Ref.7
Modified residue191Phosphothreonine Ref.7
Modified residue211Phosphoserine Ref.7
Modified residue791Phosphoserine Ref.8

Secondary structure

............................................................................................ 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32861 [UniParc].

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

FASTA49955,988
        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' 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. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"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].
[6]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"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 SER-17; THR-19 AND SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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 SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[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.
PIRS30007.
RefSeqNP_012889.3. NM_001179601.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I5KX-ray3.10A/B12-499[»]
ProteinModelPortalP32861.
SMRP32861. Positions 20-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34096. 60 interactions.
DIPDIP-4534N.
IntActP32861. 17 interactions.
MINTMINT-488090.
STRING4932.YKL035W.

Proteomic databases

MaxQBP32861.
PaxDbP32861.
PeptideAtlasP32861.
PRIDEP32861.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL035W; YKL035W; YKL035W.
GeneID853830.
KEGGsce:YKL035W.

Organism-specific databases

CYGDYKL035w.
SGDS000001518. UGP1.

Phylogenomic databases

eggNOGCOG4284.
GeneTreeENSGT00390000003174.
HOGENOMHOG000113618.
KOK00963.
OMAPPNGKRC.
OrthoDBEOG7KDFKX.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17138.
YEAST:YKL035W-MONOMER.

Gene expression databases

GenevestigatorP32861.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR029044. Nucleotide-diphossugar_trans.
IPR002618. UDPGP_trans.
IPR016267. UDPGP_trans_subgr.
[Graphical view]
PANTHERPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFPIRSF000806. UDPGP. 1 hit.
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32861.
NextBio975029.
PROP32861.

Entry information

Entry nameUGPA1_YEAST
AccessionPrimary (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: June 11, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references