Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenylosuccinate lyase

Gene

Adsl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.By similarity

Catalytic activityi

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.By similarity
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.By similarity

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 isozyme 1 (Adssl1), Adenylosuccinate synthetase isozyme 1 (Adssl1), Adenylosuccinate synthetase (Adss), Adenylosuccinate synthetase isozyme 2 (Adss), Adenylosuccinate synthetase isozyme 2 (Adss), Adenylosuccinate synthetase isozyme 1 (Adssl1)
  2. Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl)
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. Multifunctional protein ADE2 (Paics)
  2. Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl)
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 sitei159Proton donor/acceptorBy similarity1
Binding sitei241SubstrateBy similarity1
Active sitei289Proton donor/acceptorBy similarity1
Binding sitei303Substrate; shared with neighboring subunitBy similarity1
Binding sitei329SubstrateBy similarity1
Binding sitei334SubstrateBy similarity1
Binding sitei338SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2By similarity)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:Adsl
Synonyms:Adl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:103202. Adsl.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001378942 – 484Adenylosuccinate lyaseAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei9PhosphoserineBy similarity1
Modified residuei15PhosphoserineBy similarity1
Modified residuei147N6-acetyllysineBy similarity1
Modified residuei295N6-acetyllysineBy similarity1
Cross-linki415Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP54822.
MaxQBiP54822.
PaxDbiP54822.
PeptideAtlasiP54822.
PRIDEiP54822.

PTM databases

iPTMnetiP54822.
PhosphoSitePlusiP54822.
SwissPalmiP54822.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022407.
CleanExiMM_ADSL.
ExpressionAtlasiP54822. baseline and differential.
GenevisibleiP54822. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi198009. 1 interactor.
IntActiP54822. 3 interactors.
MINTiMINT-4109237.
STRINGi10090.ENSMUSP00000023043.

Structurei

3D structure databases

ProteinModelPortaliP54822.
SMRiP54822.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 21Substrate binding; shared with neighboring subunitBy similarity2
Regioni85 – 87Substrate bindingBy similarity3
Regioni111 – 112Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP54822.
KOiK01756.
OMAiWRKLWIA.
OrthoDBiEOG091G06S3.
TreeFamiTF106385.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54822-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE
60 70 80 90 100
QTLGLPITDE QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP
110 120 130 140 150
KAAGIIHLGA TSCYVGDNTD LIILRNAFDL LLPKLARVIS RLADFAKDRA
160 170 180 190 200
DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC MDLQNLKRVR DELRFRGVKG
210 220 230 240 250
TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG QTYTRKVDIE
260 270 280 290 300
VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR
310 320 330 340 350
SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT
360 370 380 390 400
ILNTLQNISE GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH
410 420 430 440 450
EKIRVLSQQA AAVVKQEGGD NDLIERIRAD AYFSPIHSQL EHLLDPSSFT
460 470 480
GRAPQQVHRF LEEEVRPLLK PYGNEMAVKA ELCL
Length:484
Mass (Da):54,866
Last modified:July 27, 2011 - v2
Checksum:i9F11689AD41D1453
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti179 – 180LC → SV in AAB60684 (PubMed:8530047).Curated2
Sequence conflicti192 – 193EL → DV in AAB60684 (PubMed:8530047).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20225 mRNA. Translation: AAB60684.1.
AK049372 mRNA. Translation: BAC33717.1.
AK051111 mRNA. Translation: BAC34529.1.
AK152092 mRNA. Translation: BAE30940.1.
AK168906 mRNA. Translation: BAE40720.1.
AK171725 mRNA. Translation: BAE42633.1.
CH466550 Genomic DNA. Translation: EDL04592.1.
BC020187 mRNA. Translation: AAH20187.1.
CCDSiCCDS27664.1.
RefSeqiNP_033764.2. NM_009634.6.
UniGeneiMm.38151.

Genome annotation databases

EnsembliENSMUST00000023043; ENSMUSP00000023043; ENSMUSG00000022407.
GeneIDi11564.
KEGGimmu:11564.
UCSCiuc007wvz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20225 mRNA. Translation: AAB60684.1.
AK049372 mRNA. Translation: BAC33717.1.
AK051111 mRNA. Translation: BAC34529.1.
AK152092 mRNA. Translation: BAE30940.1.
AK168906 mRNA. Translation: BAE40720.1.
AK171725 mRNA. Translation: BAE42633.1.
CH466550 Genomic DNA. Translation: EDL04592.1.
BC020187 mRNA. Translation: AAH20187.1.
CCDSiCCDS27664.1.
RefSeqiNP_033764.2. NM_009634.6.
UniGeneiMm.38151.

3D structure databases

ProteinModelPortaliP54822.
SMRiP54822.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198009. 1 interactor.
IntActiP54822. 3 interactors.
MINTiMINT-4109237.
STRINGi10090.ENSMUSP00000023043.

PTM databases

iPTMnetiP54822.
PhosphoSitePlusiP54822.
SwissPalmiP54822.

Proteomic databases

EPDiP54822.
MaxQBiP54822.
PaxDbiP54822.
PeptideAtlasiP54822.
PRIDEiP54822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023043; ENSMUSP00000023043; ENSMUSG00000022407.
GeneIDi11564.
KEGGimmu:11564.
UCSCiuc007wvz.2. mouse.

Organism-specific databases

CTDi158.
MGIiMGI:103202. Adsl.

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP54822.
KOiK01756.
OMAiWRKLWIA.
OrthoDBiEOG091G06S3.
TreeFamiTF106385.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
ReactomeiR-MMU-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiP54822.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022407.
CleanExiMM_ADSL.
ExpressionAtlasiP54822. baseline and differential.
GenevisibleiP54822. MM.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPUR8_MOUSE
AccessioniPrimary (citable) accession number: P54822
Secondary accession number(s): Q8VCD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.