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Protein

Adenylosuccinate lyase

Gene

adsl-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 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.
(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 (adss-1)
  2. Adenylosuccinate lyase (adsl-1)
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. Probable multifunctional protein ADE2 (B0286.3)
  2. Adenylosuccinate lyase (adsl-1)
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 sitei155 – 1551Proton donor/acceptorBy similarity
Binding sitei237 – 2371SubstrateBy similarity
Active sitei285 – 2851Proton donor/acceptorBy similarity
Binding sitei299 – 2991Substrate; shared with neighboring subunitBy similarity
Binding sitei325 – 3251SubstrateBy similarity
Binding sitei330 – 3301SubstrateBy similarity
Binding sitei334 – 3341SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiR-CEL-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:adsl-1Imported
ORF Names:R06C7.5Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiR06C7.5a; CE06248; WBGene00011064; adsl-1.
R06C7.5b; CE32476; WBGene00011064; adsl-1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Adenylosuccinate lyasePRO_0000137897Add
BLAST

Proteomic databases

EPDiQ21774.
PaxDbiQ21774.
PRIDEiQ21774.

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (Probable).1 Publication

Protein-protein interaction databases

BioGridi37909. 2 interactions.
STRINGi6239.R06C7.5a.2.

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi10 – 134Combined sources
Turni14 – 185Combined sources
Helixi21 – 244Combined sources
Helixi27 – 4721Combined sources
Helixi55 – 639Combined sources
Turni64 – 663Combined sources
Helixi70 – 7910Combined sources
Helixi83 – 9412Combined sources
Turni96 – 983Combined sources
Helixi99 – 1013Combined sources
Turni102 – 1054Combined sources
Helixi108 – 14437Combined sources
Turni145 – 1473Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi157 – 1637Combined sources
Helixi164 – 18825Combined sources
Turni196 – 1983Combined sources
Helixi202 – 2076Combined sources
Turni208 – 2103Combined sources
Helixi212 – 22514Combined sources
Beta strandi236 – 2383Combined sources
Helixi242 – 27029Combined sources
Beta strandi273 – 2753Combined sources
Helixi295 – 30814Combined sources
Helixi311 – 3199Combined sources
Helixi327 – 3293Combined sources
Helixi330 – 35728Combined sources
Helixi362 – 38423Combined sources
Turni422 – 4254Combined sources
Turni427 – 4293Combined sources
Helixi430 – 4389Combined sources
Helixi440 – 4434Combined sources
Helixi447 – 45711Combined sources
Helixi459 – 4635Combined sources
Helixi464 – 4663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YISX-ray2.40A1-478[»]
ProteinModelPortaliQ21774.
SMRiQ21774. Positions 2-468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ21774.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 152Substrate binding; shared with neighboring subunitBy similarity
Regioni81 – 833Substrate bindingBy similarity
Regioni107 – 1082Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
InParanoidiQ21774.
KOiK01756.
OMAiWRKLWIA.
PhylomeDBiQ21774.

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.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform aImported (identifier: Q21774-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASEDKFESV LSTRYCKNSP LVSILSETNK ATLWRQLWIW LAEAEKELGL
60 70 80 90 100
KQVTQDAIDE MKSNRDVFDW PFIRSEERKL KHDVMAHNHA FGKLCPTAAG
110 120 130 140 150
IIHLGATSCF VQDNADLIAY RDSIDHILKR FATVIDRLAA FSLKNKEVVT
160 170 180 190 200
VGRTHYQTAS LVTVGKRGVL WAQELLMAFQ SLSEFRDKMR FRGIKGATGT
210 220 230 240 250
QDSFLTLFAG DESKVEALDE LVTKKANFSN RFLITGQTYS RQQDSQLVFS
260 270 280 290 300
LSLLGAAAKK VCTDIRVLQA FGELLEPFEK DQIGSSAMPY KKNPMKSERC
310 320 330 340 350
CALSRKLINA PQEALTILAD QGLERTLDDS AGRRMLIPDV LLTAEALLTT
360 370 380 390 400
LQNIFEGLSV QTDNVKKIVE DEIAFLGLEK AMMMLTEEGV DRQQAHAVIR
410 420 430 440 450
KTALEAKQLQ ATQKVDIRQT MADPFFDSVR DRVVGLVNNP INFTGRCVSQ
460 470
TESFIAKELK PTIDKYLDKS AGNVQLDV
Length:478
Mass (Da):53,569
Last modified:November 1, 1996 - v1
Checksum:i0E7FAA122D32774F
GO
Isoform bImported (identifier: Q21774-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     353-370: NIFEGLSVQTDNVKKIVE → VSVLKITSSKDLVYKQTM
     371-478: Missing.

Note: No experimental confirmation available.
Show »
Length:370
Mass (Da):41,496
Checksum:iC803E93C6C048BA1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei353 – 37018NIFEG…KKIVE → VSVLKITSSKDLVYKQTM in isoform b. CuratedVSP_016396Add
BLAST
Alternative sequencei371 – 478108Missing in isoform b. CuratedVSP_016397Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71266 Genomic DNA. Translation: CAA95843.1.
Z71266 Genomic DNA. Translation: CAD56593.1.
PIRiT23969.
RefSeqiNP_492049.1. NM_059648.5. [Q21774-1]
NP_871850.1. NM_182050.3. [Q21774-2]
UniGeneiCel.157.

Genome annotation databases

EnsemblMetazoaiR06C7.5a; R06C7.5a; WBGene00011064. [Q21774-1]
GeneIDi172466.
KEGGicel:CELE_R06C7.5.
UCSCiR06C7.5a. c. elegans. [Q21774-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71266 Genomic DNA. Translation: CAA95843.1.
Z71266 Genomic DNA. Translation: CAD56593.1.
PIRiT23969.
RefSeqiNP_492049.1. NM_059648.5. [Q21774-1]
NP_871850.1. NM_182050.3. [Q21774-2]
UniGeneiCel.157.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YISX-ray2.40A1-478[»]
ProteinModelPortaliQ21774.
SMRiQ21774. Positions 2-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi37909. 2 interactions.
STRINGi6239.R06C7.5a.2.

Proteomic databases

EPDiQ21774.
PaxDbiQ21774.
PRIDEiQ21774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiR06C7.5a; R06C7.5a; WBGene00011064. [Q21774-1]
GeneIDi172466.
KEGGicel:CELE_R06C7.5.
UCSCiR06C7.5a. c. elegans. [Q21774-1]

Organism-specific databases

CTDi172466.
WormBaseiR06C7.5a; CE06248; WBGene00011064; adsl-1.
R06C7.5b; CE32476; WBGene00011064; adsl-1.

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
InParanoidiQ21774.
KOiK01756.
OMAiWRKLWIA.
PhylomeDBiQ21774.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ21774.
NextBioi875631.
PROiQ21774.

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.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: Bristol N2.
  2. "Structural genomics of Caenorhabditis elegans: adenylosuccinate lyase."
    Southeast collaboratory for structural genomics (SECSG)
    Submitted (FEB-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiPUR8_CAEEL
AccessioniPrimary (citable) accession number: Q21774
Secondary accession number(s): Q8I4G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.