Adenylosuccinate lyase - Mus musculus (Mouse)

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P54822 (PUR8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Adenylosuccinate lyase
Short name=ASL
EC=4.3.2.2

Alternative name(s):
Adenylosuccinase
Short name=ASase

Gene names

Name:	Adsl
Synonyms:	Adl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 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.
Subunit structure	Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site By similarity.
Sequence similarities	Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Lyase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' AMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway AMP biosynthetic process Inferred from sequence alignment PubMed 8995283. Source: MGI aerobic respiration Inferred from electronic annotation. Source: Compara protein tetramerization Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to muscle activity Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara response to starvation Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI
Molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Inferred from sequence alignment PubMed 8995283. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 484

483

Adenylosuccinate lyase

PRO_0000137894

Regions

Region

20 – 21

Substrate binding; shared with neighboring subunit By similarity

Region

85 – 87

Substrate binding By similarity

Region

111 – 112

Substrate binding By similarity

Sites

Active site

159

Proton donor/acceptor By similarity

Active site

289

Proton donor/acceptor By similarity

Binding site

241

Substrate By similarity

Binding site

303

Substrate; shared with neighboring subunit By similarity

Binding site

329

Substrate By similarity

Binding site

334

Substrate By similarity

Binding site

338

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

147

N6-acetyllysine By similarity

Modified residue

295

N6-acetyllysine By similarity

Experimental info

Sequence conflict

179 – 180

LC → SV in AAB60684. Ref.1

Sequence conflict

192 – 193

EL → DV in AAB60684. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P54822 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 9F11689AD41D1453
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FASTA

484

54,866

        10         20         30         40         50         60 
MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE QTLGLPITDE 

        70         80         90        100        110        120 
QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD 

       130        140        150        160        170        180 
LIILRNAFDL LLPKLARVIS RLADFAKDRA DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC 

       190        200        210        220        230        240 
MDLQNLKRVR DELRFRGVKG TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG 

       250        260        270        280        290        300 
QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR 

       310        320        330        340        350        360 
SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE 

       370        380        390        400        410        420 
GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH EKIRVLSQQA AAVVKQEGGD 

       430        440        450        460        470        480 
NDLIERIRAD AYFSPIHSQL EHLLDPSSFT GRAPQQVHRF LEEEVRPLLK PYGNEMAVKA 


ELCL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the cDNA and the gene encoding murine adenylosuccinate lyase." Wong L.J., O'Brien W.E. Genomics 28:341-343(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129. Tissue: Kidney.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Kidney and Spleen.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Salivary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00308217.
RefSeq	NP_033764.2. NM_009634.6.
UniGene	Mm.38151.
3D structure databases
HSSP	HSSP built from PDB template 1DOF based on UniProtKB Q8ZY28.
ProteinModelPortal	P54822.
SMR	P54822. Positions 5-472.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000023043.
PTM databases
PhosphoSite	P54822.
Proteomic databases
PaxDb	P54822.
PRIDE	P54822.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023043; ENSMUSP00000023043; ENSMUSG00000022407.
GeneID	11564.
KEGG	mmu:11564.
Organism-specific databases
CTD	158.
MGI	MGI:103202. Adsl.
Phylogenomic databases
eggNOG	COG0015.
GeneTree	ENSGT00390000013486.
HOGENOM	HOG000033915.
HOVERGEN	HBG000214.
InParanoid	Q8VCD4.
KO	K01756.
OMA	PVLGWTH.
OrthoDB	EOG4QJRN2.
Enzyme and pathway databases
UniPathway	UPA00074; UER00132. UPA00075; UER00336.
Gene expression databases
ArrayExpress	P54822.
Bgee	P54822.
CleanEx	MM_ADSL.
Genevestigator	P54822.
GermOnline	ENSMUSG00000022407. Mus musculus.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
InterPro	IPR019468. AdenyloSucc_lyase_C. IPR003031. D_crystallin. IPR024083. Fumarase/histidase_N. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. IPR004769. Pur_lyase. [Graphical view]
PANTHER	PTHR11444:SF2. PTHR11444:SF2. 1 hit.
Pfam	PF10397. ADSL_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
SMART	SM00998. ADSL_C. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00928. purB. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	279062.
SOURCE	Search...

Entry information

Entry name

PUR8_MOUSE

Accession

Primary (citable) accession number: P54822
Secondary accession number(s): Q8VCD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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

PTM 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