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P54822 (PUR8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Adsl
Synonyms:Adl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 484483Adenylosuccinate lyase
PRO_0000137894

Regions

Region20 – 212Substrate binding; shared with neighboring subunit By similarity
Region85 – 873Substrate binding By similarity
Region111 – 1122Substrate binding By similarity

Sites

Active site1591Proton donor/acceptor By similarity
Active site2891Proton donor/acceptor By similarity
Binding site2411Substrate By similarity
Binding site3031Substrate; shared with neighboring subunit By similarity
Binding site3291Substrate By similarity
Binding site3341Substrate By similarity
Binding site3381Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1471N6-acetyllysine By similarity
Modified residue2951N6-acetyllysine By similarity

Experimental info

Sequence conflict179 – 1802LC → SV in AAB60684. Ref.1
Sequence conflict192 – 1932EL → DV in AAB60684. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54822 [UniParc].

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

FASTA48454,866
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
CCDSCCDS27664.1.
RefSeqNP_033764.2. NM_009634.6.
UniGeneMm.38151.

3D structure databases

ProteinModelPortalP54822.
SMRP54822. Positions 5-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198009. 1 interaction.
IntActP54822. 3 interactions.
MINTMINT-4109237.
STRING10090.ENSMUSP00000023043.

PTM databases

PhosphoSiteP54822.

Proteomic databases

MaxQBP54822.
PaxDbP54822.
PRIDEP54822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023043; ENSMUSP00000023043; ENSMUSG00000022407.
GeneID11564.
KEGGmmu:11564.
UCSCuc007wvz.1. mouse.

Organism-specific databases

CTD158.
MGIMGI:103202. Adsl.

Phylogenomic databases

eggNOGCOG0015.
GeneTreeENSGT00390000013486.
HOGENOMHOG000033915.
HOVERGENHBG000214.
InParanoidQ8VCD4.
KOK01756.
OMAMAHVHAY.
OrthoDBEOG7GQXVD.
TreeFamTF106385.

Enzyme and pathway databases

UniPathwayUPA00074; UER00132.
UPA00075; UER00336.

Gene expression databases

ArrayExpressP54822.
BgeeP54822.
CleanExMM_ADSL.
GenevestigatorP54822.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
InterProIPR019468. 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]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SMARTSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00928. purB. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279062.
PROP54822.
SOURCESearch...

Entry information

Entry namePUR8_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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