Adenine phosphoribosyltransferase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P49435 (APT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 123. History...

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

Documents (5) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Adenine phosphoribosyltransferase 1
Short name=APRT 1
EC=2.4.2.7

Gene names

Name:	APT1
Ordered Locus Names:	YML022W

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	187 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Ref.7
Catalytic activity	AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate.
Cofactor	Magnesium. Ref.6
Pathway	Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subunit structure	Homodimer. Ref.6 Ref.7 Ref.11
Subcellular location	Cytoplasm. Nucleus Ref.8.
Miscellaneous	Present with 11200 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
Biological process	Purine salvage
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	AMP biosynthetic process Traceable author statement Ref.6. Source: SGD AMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway adenine salvage Inferred from mutant phenotype Ref.7. Source: SGD purine ribonucleoside salvage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: SGD nucleus Inferred from direct assay Ref.8. Source: SGD
Molecular_function	adenine phosphoribosyltransferase activity Inferred from direct assay Ref.7. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 187

187

Adenine phosphoribosyltransferase 1

PRO_0000149517

Regions

Nucleotide binding

133 – 137

AMP Probable

Amino acid modifications

Modified residue

Phosphoserine Ref.10

Experimental info

Mutagenesis

R → A: 4-fold decrease in activity. Ref.11

Mutagenesis

R → A: 2-fold decrease in activity. Ref.11

Mutagenesis

K → A: 30-fold decrease in activity. Ref.11

Mutagenesis

K → A: Small increase in activity. Ref.11

Mutagenesis

103

Y → F: 4-fold increase in activity. Ref.11

Mutagenesis

106

E → L: 1 million-fold decrease in activity. Ref.11

Mutagenesis

106

E → Q: 2-fold decrease in activity. Ref.11

Mutagenesis

107

Y → D: 2/3-fold decrease in activity. Ref.11

Mutagenesis

107

Y → F: Small decrease in activity. Ref.11

Mutagenesis

108

G → A: Small decrease in activity. Ref.11

Mutagenesis

108

G → H: 2/3-fold decrease in activity. Ref.11

Sequence conflict

P → F in AAA89075. Ref.1

Secondary structure

187

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P49435 [UniParc].

Last modified February 21, 2006. Version 3.
Checksum: 68061D4BAA42EDEF
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FASTA

187

20,587

        10         20         30         40         50         60 
MSIASYAQEL KLALHQYPNF PSEGILFEDF LPIFRNPGLF QKLIDAFKLH LEEAFPEVKI 

        70         80         90        100        110        120 
DYIVGLESRG FLFGPTLALA LGVGFVPVRK AGKLPGECFK ATYEKEYGSD LFEIQKNAIP 

       130        140        150        160        170        180 
AGSNVIIVDD IIATGGSAAA AGELVEQLEA NLLEYNFVME LDFLKGRSKL NAPVFTLLNA 


QKEALKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the adenine phosphoribosyltransferase-encoding gene (APT1) from Saccharomyces cerevisiae." Alfonzo J.D., Sahota A., Deeley M.C., Ranjekar P., Taylor M.W. Gene 161:81-85(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DS1.
[2]	Taylor M.W., Alfonzo J.D. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Purification and characterization of adenine phosphoribosyltransferase from Saccharomyces cerevisiae." Alfonzo J.D., Sahota A., Taylor M.W. Biochim. Biophys. Acta 1341:173-182(1997) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR, SUBUNIT. Strain: ATCC 24903.
[7]	"APT1, but not APT2, codes for a functional adenine phosphoribosyltransferase in Saccharomyces cerevisiae." Alfonzo J.D., Crother T.R., Guetsova M.L., Daignan-Fornier B., Taylor M.W. J. Bacteriol. 181:347-352(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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].
[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 SER-68, MASS SPECTROMETRY.
[11]	"Structural analysis of adenine phosphoribosyltransferase from Saccharomyces cerevisiae." Shi W., Tanaka K.S.E., Crother T.R., Taylor M.W., Almo S.C., Schramm V.L. Biochemistry 40:10800-10809(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 3-187 OF APOENZYME AND IN COMPLEX WITH SUBSTRATE ANALOG, HOMODIMERIZATION, MUTAGENESIS OF ARG-69; ARG-89; LYS-90; LYS-93; TYR-103; GLU-106; TYR-107 AND GLY-108.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U16781 Genomic DNA. Translation: AAA89075.1.
Z46659 Genomic DNA. Translation: CAA86633.1.
AY558232 Genomic DNA. Translation: AAS56558.1.
BK006946 Genomic DNA. Translation: DAA09876.1.

PIR

S49755.

RefSeq

NP_013690.1. NM_001182380.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G2P	X-ray	1.75	A	3-187	[»]
1G2Q	X-ray	1.50	A/B	3-187	[»]

ProteinModelPortal

P49435.

SMR

P49435. Positions 1-178.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2057N.

IntAct

P49435. 2 interactions.

MINT

MINT-504301.

STRING

4932.YML022W.

Proteomic databases

PaxDb

P49435.

PeptideAtlas

P49435.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YML022W; YML022W; YML022W.

GeneID

854986.

KEGG

sce:YML022W.

Organism-specific databases

CYGD

YML022w.

SGD

S000004484. APT1.

Phylogenomic databases

eggNOG

COG0503.

GeneTree

ENSGT00390000017259.

HOGENOM

HOG000036776.

K00759.

OMA

RYKDQGI.

OrthoDB

EOG4M3DK3.

Enzyme and pathway databases

BioCyc

MetaCyc:YML022W-MONOMER.

UniPathway

UPA00588; UER00646.

Gene expression databases

Genevestigator

P49435.

GermOnline

YML022W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005764. Ade_phspho_trans.
IPR000836. PRibTrfase_dom.
[Graphical view]

Pfam

PF00156. Pribosyltran. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01090. apt. 1 hit.

PROSITE

PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P49435.

NextBio

978115.

Entry information

Entry name

APT1_YEAST

Accession

Primary (citable) accession number: P49435
Secondary accession number(s): D6VZF2, Q6Q5A3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 21, 2006
Last modified:	April 3, 2013
This is version 123 of the entry and version 3 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 XIII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

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