Adenylosuccinate synthetase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P80210 (PURA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 114. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Adenylosuccinate synthetase
Short name=AMPSase
Short name=AS-synthetase
Short name=AdSS
EC=6.3.4.4

Alternative name(s):
IMP--aspartate ligase

Gene names

Name:	ADE12
Ordered Locus Names:	YNL220W
ORF Names:	N1290

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP. Ref.6 Ref.7
Catalytic activity	GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Enzyme regulation	Inhibited by GMP. Inhibited by chloride. Inhibited in a highly specific manner by the binding of a 44-base DNA oligonucleotide carrying the ARS core consensus sequence. Ref.6
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subunit structure	Homodimer. Ref.2 Ref.6 Ref.7
Subcellular location	Cytoplasm Ref.8.
Miscellaneous	Present with 56800 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the adenylosuccinate synthetase family.
Biophysicochemical properties	Kinetic parameters: K_M=1650 µM for L-aspartate Ref.6 Ref.7 K_M=200 µM for IMP K_M=1650 µM for GTP pH dependence: Optimum pH is 8.0. Temperature dependence: Optimum temperature is 35 degrees Celsius.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay Ref.8. Source: SGD
Molecular function	DNA replication origin binding Inferred from direct assay Ref.2. Source: SGD GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylosuccinate synthase activity Inferred from direct assay Ref.6 Ref.2. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRP40	P33203	2	EBI-14267,EBI-701
RSP5	P39940	2	EBI-14267,EBI-16219

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5 Ref.6

Chain

2 – 433

432

Adenylosuccinate synthetase

PRO_0000095138

Regions

Nucleotide binding

11 – 17

GTP By similarity

Nucleotide binding

39 – 41

GTP By similarity

Nucleotide binding

337 – 339

GTP By similarity

Nucleotide binding

419 – 421

GTP By similarity

Region

12 – 15

IMP binding By similarity

Region

37 – 40

IMP binding By similarity

Region

305 – 311

Substrate binding By similarity

Sites

Active site

Proton acceptor By similarity

Active site

Proton donor By similarity

Metal binding

Magnesium By similarity

Metal binding

Magnesium; via carbonyl oxygen By similarity

Binding site

134

IMP By similarity

Binding site

148

IMP; shared with dimeric partner By similarity

Binding site

230

IMP By similarity

Binding site

245

IMP By similarity

Binding site

309

IMP By similarity

Binding site

311

GTP By similarity

Amino acid modifications

Modified residue

122

Phosphoserine Ref.10

Modified residue

143

Phosphoserine Ref.10

Experimental info

Sequence conflict

237

D → G AA sequence Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P80210 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 800E0F4062D9856F
Show »

FASTA

433

48,279

        10         20         30         40         50         60 
MVNVVLGSQW GDEGKGKLVD LLVGKYDIVA RCAGGNNAGH TIVVDGVKYD FHMLPSGLVN 

        70         80         90        100        110        120 
PNCQNLLGNG VVIHVPSFFK ELETLEAKGL KNARSRLFVS SRAHLVFDFH QVTDKLRELE 

       130        140        150        160        170        180 
LSGRSKDGKN IGTTGKGIGP TYSTKASRSG LRVHHLVNDQ PGAWEEFVAR YKRLLETRRQ 

       190        200        210        220        230        240 
RYGDFEYDFE AKLAEYKKLR EQLKPFVVDS VVFMHNAIEA KKKILVEGAN ALMLDIDFGT 

       250        260        270        280        290        300 
YPYVTSSNTG IGGVLTGLGI PPRTIDEIYG VVKAYTTRVG EGPFPTEQLN ENGEKLQTIG 

       310        320        330        340        350        360 
AEFGVTTGRK RRCGWLDLVV LKYSTLINGY TSLNITKLDV LDTFKEIPVG ISYSIQGKKL 

       370        380        390        400        410        420 
DLFPEDLNIL GKVEVEYKVL PGWDQDITKI TKYEDLPENA KKYLKYIEDF VGVPVEWVGT 

       430 
GPARESMLHK EIK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Saccharomyces cerevisiae ADE12 gene, coding for adenylosuccinate synthetase (EC 6.3.4.4). Cloning, sequencing, expression, and superproduction." Andreichuk I.V., Shabes A.V., Ryzhova T.A., Kotova I.A., Domkin V.D. Mol. Genet. Mikrobiol. Virusol. 1:21-28(1995) [PubMed: 7603488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Enzymatic properties and inhibition by single-stranded autonomously replicating sequences of adenylosuccinate synthase from Saccharomyces cerevisiae." Gallert K.C., Ohanjan T., Daignan-Fornier B., Lottspeich F., Krauss G. Eur. J. Biochem. 239:487-493(1996) [PubMed: 8706758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INHIBITION BY SS-DNA, SUBUNIT.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Characterization of two novel single-stranded DNA-specific autonomously replicating sequence-binding proteins from Saccharomyces cerevisiae, one of which is adenylosuccinate synthetase." Zeidler R., Hobert O., Johannes L., Faulhammer H., Krauss G. J. Biol. Chem. 268:20191-20197(1993) [PubMed: 8376380] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-23 AND 234-245.
[6]	"Adenylosuccinate synthase from Saccharomyces cerevisiae: homologous overexpression, purification and characterization of the recombinant protein." Lipps G., Krauss G. Biochem. J. 341:537-543(1999) [PubMed: 10417315] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
[7]	"Adenylosuccinate synthetase of the yeast Saccharomyces cerevisiae: purification and properties." Ryzhova T.A., Andreichuk Y.V., Domkin V.D. Biokhimiia 63:650-656(1998) [PubMed: 9668204] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, 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: 14562095] [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: 14562106] [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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-143, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L22185 Genomic DNA. Translation: AAA91338.1. Z48671 Genomic DNA. Translation: CAA88590.1. Z71496 Genomic DNA. Translation: CAA96123.1. BK006947 Genomic DNA. Translation: DAA10336.1.
PIR	S48515.
RefSeq	NP_014179.1. NM_001183058.1.
3D structure databases
ProteinModelPortal	P80210.
SMR	P80210. Positions 1-430.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4286N.
IntAct	P80210. 10 interactions.
MINT	MINT-560386.
STRING	P80210.
Proteomic databases
PeptideAtlas	P80210.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL220W; YNL220W; YNL220W.
GeneID	855501.
KEGG	sce:YNL220W.
NMPDR	fig\|4932.3.peg.5244.
Organism-specific databases
SGD	S000005164. ADE12.
Phylogenomic databases
eggNOG	fuNOG05044.
GeneTree	EFGT00050000004457.
HOGENOM	HBG658237.
OMA	DYVVRYQ.
OrthoDB	EOG4S4SQR.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-509.
Gene expression databases
ArrayExpress	P80210.
Genevestigator	P80210.
GermOnline	YNL220W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view]
KO	K01939.
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
SMART	SM00788. Adenylsucc_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR00184. PurA. 1 hit.
PROSITE	PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979499.

Entry information

Entry name

PURA_YEAST

Accession

Primary (citable) accession number: P80210
Secondary accession number(s): D6W0X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 114 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 XIV

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

Experimental info

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