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Protein

Adenylosuccinate lyase

Gene

ADE13

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

N6-(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.

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes AMP from IMP.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase (ADE12)
  2. Adenylosuccinate lyase (ADE13)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylaminoimidazole-succinocarboxamide synthase (ADE1)
  2. Adenylosuccinate lyase (ADE13)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei156Proton donor/acceptorBy similarity1
Binding sitei238SubstrateBy similarity1
Active sitei286Proton donor/acceptorBy similarity1
Binding sitei300Substrate; shared with neighboring subunitBy similarity1
Binding sitei326SubstrateBy similarity1
Binding sitei331SubstrateBy similarity1
Binding sitei335SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • 'de novo' AMP biosynthetic process Source: GO_Central
  • 'de novo' IMP biosynthetic process Source: SGD
  • purine nucleotide biosynthetic process Source: SGD

Keywordsi

Molecular functionLyase
Biological processPurine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:YLR359W-MONOMER
YEAST:YLR359W-MONOMER
ReactomeiR-SCE-73817 Purine ribonucleoside monophosphate biosynthesis
UniPathwayiUPA00074; UER00132
UPA00075; UER00336

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:ADE13
Ordered Locus Names:YLR359W
ORF Names:L8039.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR359W
SGDiS000004351 ADE13

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001378991 – 482Adenylosuccinate lyaseAdd BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ05911
PaxDbiQ05911
PRIDEiQ05911

PTM databases

iPTMnetiQ05911

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PRT1P061032EBI-14263,EBI-8973

Protein-protein interaction databases

BioGridi31620, 54 interactors
DIPiDIP-2787N
IntActiQ05911, 6 interactors
MINTiQ05911
STRINGi4932.YLR359W

Structurei

3D structure databases

ProteinModelPortaliQ05911
SMRiQ05911
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 15Substrate binding; shared with neighboring subunitBy similarity2
Regioni82 – 84Substrate bindingBy similarity3
Regioni108 – 109Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000013486
HOGENOMiHOG000033915
InParanoidiQ05911
KOiK01756
OMAiASSCEKI
OrthoDBiEOG092C1WGC

Family and domain databases

InterProiView protein in InterPro
IPR019468 AdenyloSucc_lyase_C
IPR020557 Fumarate_lyase_CS
IPR000362 Fumarate_lyase_fam
IPR022761 Fumarate_lyase_N
IPR008948 L-Aspartase-like
IPR004769 Pur_lyase
PfamiView protein in Pfam
PF10397 ADSL_C, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SMARTiView protein in SMART
SM00998 ADSL_C, 1 hit
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR00928 purB, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 1 hit

Sequencei

Sequence statusi: Complete.

Q05911-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDYDNYTTP LSSRYASKEM SATFSLRNRF STWRKLWLNL AIAEKELGLT
60 70 80 90 100
VVTDEAIEQM RKHVEITDDE IAKASAQEAI VRHDVMAHVH TFGETCPAAA
110 120 130 140 150
GIIHLGATSC FVTDNADLIF IRDAYDIIIP KLVNVINRLA KFAMEYKDLP
160 170 180 190 200
VLGWTHFQPA QLTTLGKRAT LWIQELLWDL RNFERARNDI GLRGVKGTTG
210 220 230 240 250
TQASFLALFH GNHDKVEALD ERVTELLGFD KVYPVTGQTY SRKIDIDVLA
260 270 280 290 300
PLSSFAATAH KMATDIRLLA NLKEVEEPFE KSQIGSSAMA YKRNPMRCER
310 320 330 340 350
VCSLARHLGS LFSDAVQTAS VQWFERTLDD SAIRRISLPS AFLTADILLS
360 370 380 390 400
TLLNISSGLV VYPKVIERRI KGELPFMATE NIIMAMVEKN ASRQEVHERI
410 420 430 440 450
RVLSHQAAAV VKEEGGENDL IERVKRDEFF KPIWEELDSL LEPSTFVGRA
460 470 480
PQQVEKFVQK DVNNALQPFQ KYLNDEQVKL NV
Length:482
Mass (Da):54,510
Last modified:November 1, 1996 - v1
Checksum:iAED9468B7828AB77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19103 Genomic DNA Translation: AAB67573.1
U19102 Genomic DNA Translation: AAB67755.2
BK006945 Genomic DNA Translation: DAA09662.1
PIRiS51377
RefSeqiNP_013463.1, NM_001182248.1

Genome annotation databases

EnsemblFungiiYLR359W; YLR359W; YLR359W
GeneIDi851073
KEGGisce:YLR359W

Similar proteinsi

Entry informationi

Entry nameiPUR8_YEAST
AccessioniPrimary (citable) accession number: Q05911
Secondary accession number(s): D6VYZ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 165 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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