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Protein

Adenylosuccinate lyase

Gene

ADSL

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 2 (ADSS), Adenylosuccinate synthetase isozyme 1 (ADSSL1)
  2. 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. no protein annotated in this organism
  2. 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651Proton donor/acceptorBy similarity
Binding sitei247 – 2471SubstrateBy similarity
Active sitei295 – 2951Proton donor/acceptorBy similarity
Binding sitei309 – 3091Substrate; shared with neighboring subunitBy similarity
Binding sitei335 – 3351SubstrateBy similarity
Binding sitei340 – 3401SubstrateBy similarity
Binding sitei344 – 3441SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2By similarity)
Short name:
ADSL
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:ADSL
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 490489Adenylosuccinate lyasePRO_0000328544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei153 – 1531N6-acetyllysineBy similarity
Modified residuei301 – 3011N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiA3KN12.
PRIDEiA3KN12.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000085.

Structurei

3D structure databases

ProteinModelPortaliA3KN12.
SMRiA3KN12. Positions 17-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 272Substrate binding; shared with neighboring subunitBy similarity
Regioni91 – 933Substrate bindingBy similarity
Regioni117 – 1182Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiA3KN12.
KOiK01756.

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.

A3KN12-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGDRGGR EAACGHDSYR SPLASRYASP EMCFLFSDKY KFRTWRQLWL
60 70 80 90 100
WLAEAEQTLG LPITDEQIQE MKSNLDNIDF RMAAEEEKQL RHDVMAHVHT
110 120 130 140 150
FAHCCPKAAS IIHLGATSCY VGDNTDLIIL RNAFDLLLPK LARVISRLAD
160 170 180 190 200
FAKEQADLPT LGFTHFQPAQ LTTVGKRCCL WIQDLCMDLQ NLKRVRDELR
210 220 230 240 250
FRGVKGTTGT QASFLQLFEG DDQKVEQLDK MVTEKAGFKR AFIITGQTYT
260 270 280 290 300
RKVDIEVLSV LASLGASVHK ICTDIRLLAN LKEMEEPFEK QQIGSSAMPY
310 320 330 340 350
KRNPMRSERC CSLARHLMAL VMDPLQTASV QWFERTLDDS ANRRICLAEA
360 370 380 390 400
FLTADTVLNT LQNISEGLVV YPKVIERRVQ QELPFMATEN IIMAMVKAGG
410 420 430 440 450
NRQDCREKIR VLSQQAAAVV KQEGGDNDLI ERIQADAYFS PIHSQLDHLL
460 470 480 490
DPSSFTGRAS QQVQRFLEEE VCPLLKPYES VMKVKAELRL
Length:490
Mass (Da):55,484
Last modified:April 3, 2007 - v1
Checksum:iDB7239E73B710011
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133474 mRNA. Translation: AAI33475.1.
RefSeqiNP_001095847.1. NM_001102377.2.
UniGeneiBt.11346.

Genome annotation databases

GeneIDi510949.
KEGGibta:510949.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133474 mRNA. Translation: AAI33475.1.
RefSeqiNP_001095847.1. NM_001102377.2.
UniGeneiBt.11346.

3D structure databases

ProteinModelPortaliA3KN12.
SMRiA3KN12. Positions 17-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000085.

Proteomic databases

PaxDbiA3KN12.
PRIDEiA3KN12.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi510949.
KEGGibta:510949.

Organism-specific databases

CTDi158.

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiA3KN12.
KOiK01756.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Miscellaneous databases

NextBioi20869695.

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...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal spinal cord.

Entry informationi

Entry nameiPUR8_BOVIN
AccessioniPrimary (citable) accession number: A3KN12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 3, 2007
Last modified: January 20, 2016
This is version 60 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.