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Q05911 (PUR8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylosuccinate lyase
Short name=ASL
EC=4.3.2.2
Alternative name(s):
Adenylosuccinase
Short name=ASase
Gene names
Name:ADE13
Ordered Locus Names:YLR359W
ORF Names:L8039.12
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.

(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.

Sequence similarities

Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Adenylosuccinate lyase
PRO_0000137899

Sites

Active site831Proton donor By similarity
Active site1561Proton acceptor By similarity

Amino acid modifications

Modified residue41Phosphotyrosine Ref.4
Modified residue91Phosphothreonine Ref.4
Cross-link196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q05911 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AED9468B7828AB77

FASTA48254,510
        10         20         30         40         50         60 
MPDYDNYTTP LSSRYASKEM SATFSLRNRF STWRKLWLNL AIAEKELGLT VVTDEAIEQM 

        70         80         90        100        110        120 
RKHVEITDDE IAKASAQEAI VRHDVMAHVH TFGETCPAAA GIIHLGATSC FVTDNADLIF 

       130        140        150        160        170        180 
IRDAYDIIIP KLVNVINRLA KFAMEYKDLP VLGWTHFQPA QLTTLGKRAT LWIQELLWDL 

       190        200        210        220        230        240 
RNFERARNDI GLRGVKGTTG TQASFLALFH GNHDKVEALD ERVTELLGFD KVYPVTGQTY 

       250        260        270        280        290        300 
SRKIDIDVLA PLSSFAATAH KMATDIRLLA NLKEVEEPFE KSQIGSSAMA YKRNPMRCER 

       310        320        330        340        350        360 
VCSLARHLGS LFSDAVQTAS VQWFERTLDD SAIRRISLPS AFLTADILLS TLLNISSGLV 

       370        380        390        400        410        420 
VYPKVIERRI KGELPFMATE NIIMAMVEKN ASRQEVHERI RVLSHQAAAV VKEEGGENDL 

       430        440        450        460        470        480 
IERVKRDEFF KPIWEELDSL LEPSTFVGRA PQQVEKFVQK DVNNALQPFQ KYLNDEQVKL 


NV

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196, MASS SPECTROMETRY.
Strain: SUB592.
[4]"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 TYR-4 AND THR-9, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U19103 Genomic DNA. Translation: AAB67573.1.
U19102 Genomic DNA. Translation: AAB67755.2.
BK006945 Genomic DNA. Translation: DAA09662.1.
PIRS51377.
RefSeqNP_013463.1. NM_001182248.1.

3D structure databases

ProteinModelPortalQ05911.
SMRQ05911. Positions 5-470.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2787N.
IntActQ05911. 8 interactions.
MINTMINT-649696.
STRINGQ05911.

Proteomic databases

PeptideAtlasQ05911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR359W; YLR359W; YLR359W.
GeneID851073.
KEGGsce:YLR359W.
NMPDRfig|4932.3.peg.4485.

Organism-specific databases

CYGDYLR359w.
SGDS000004351. ADE13.

Phylogenomic databases

eggNOGfuNOG07727.
GeneTreeEFGT00050000004719.
HOGENOMHBG302411.
OMANRQDCHE.
OrthoDBEOG4WT0JV.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-489.

Gene expression databases

ArrayExpressQ05911.
GenevestigatorQ05911.
GermOnlineYLR359W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR019468. AdenyloSucc_lyase_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
IPR004769. Pur_lyase.
[Graphical view]
Gene3DG3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KOK01756.
PANTHERPTHR11444:SF2. PTHR11444:SF2. 1 hit.
PfamPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SMARTSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR00928. PurB. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967720.

Entry information

Entry namePUR8_YEAST
AccessionPrimary (citable) accession number: Q05911
Secondary accession number(s): D6VYZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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