Adenylosuccinate synthetase - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P80210 (PURA_YEAST)

Last modified November 25, 2008. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Adenylosuccinate synthetase
      Short name=AdSS
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
    AMPSase

Gene names

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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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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.

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General annotation (Comments)

Function	Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
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 in a highly specific manner by the binding of a 44-base DNA oligonucleotide carrying the ARS core consensus sequence.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subunit structure	Homodimer By similarity.
Miscellaneous	Present with 56800 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the adenylosuccinate synthetase family.

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Ontologies

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

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-14267,EBI-14267
	P43582	1	EBI-14267,EBI-22766
AUS1	Q08409	1	EBI-14267,EBI-35723
ESS1	P22696	1	EBI-14267,EBI-6679
PRP40	P33203	1	EBI-14267,EBI-701
RSP5	P39940	1	EBI-14267,EBI-16219
SET2	P46995	1	EBI-14267,EBI-16985
SSM4	P40318	1	EBI-14267,EBI-18208
URN1	Q06525	1	EBI-14267,EBI-35138

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 433

432

Adenylosuccinate synthetase

PRO_0000095138

Regions

Nucleotide binding

11 – 17

GTP By similarity

Sites

Active site

145

By similarity

Active site

152

By similarity

Metal binding

Magnesium By similarity

Metal binding

Magnesium; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

122

Phosphoserine

Modified residue

143

Phosphoserine

Experimental info

Sequence conflict

237

D → G AA sequence Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P80210-1 [UniParc].

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

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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.
[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]	"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.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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.

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Cross-references

Sequence databases
	L22185 Genomic DNA. Translation: AAA91338.1. Z48671 Genomic DNA. Translation: CAA88590.1. Z71496 Genomic DNA. Translation: CAA96123.1.
PIR	S48515.
RefSeq	NP_014179.1.
3D structure databases
HSSP	HSSP built from PDB template 1IWE based on UniProtKB P28650.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4286N.
IntAct	P80210.
Proteomic databases
PeptideAtlas	P80210.
Genome annotation databases
Ensembl	YNL220W. Saccharomyces cerevisiae. [Contig view]
GeneID	855501.
GenomeReviews	Gene locus YNL220W in contig Y13139_GR.
KEGG	sce:YNL220W.
NMPDR	fig\|4932.3.peg.5244.
Organism-specific databases
CYGD	YNL220w.
SGD	S000005164. ADE12.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P80210.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-509.
Gene expression databases
ArrayExpress	P80210.
GermOnline	YNL220W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001114. AdlSucc_Synth. [Graphical view]
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
ProDom	PD001188. Asucc_synthtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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 Resources
LinkHub	P80210.
NextBio	979499.

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Entry information

Entry name

PURA_YEAST

Accession

Primary (citable) accession number: P80210

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIV

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents