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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)DescriptionActionsGraphical viewLength
Active sitei155Proton donor/acceptorBy similarity1
Binding sitei237SubstrateBy similarity1
Active sitei285Proton donor/acceptorBy similarity1
Binding sitei299Substrate; shared with neighboring subunitBy similarity1
Binding sitei325SubstrateBy similarity1
Binding sitei330SubstrateBy similarity1
Binding sitei334SubstrateBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001378971 – 478Adenylosuccinate lyaseAdd BLAST478

Proteomic databases

EPDiQ21774.
PaxDbiQ21774.
PeptideAtlasiQ21774.
PRIDEiQ21774.

Expressioni

Gene expression databases

BgeeiWBGene00011064.

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 interactors.
STRINGi6239.R06C7.5a.2.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Helixi10 – 13Combined sources4
Turni14 – 18Combined sources5
Helixi21 – 24Combined sources4
Helixi27 – 47Combined sources21
Helixi55 – 63Combined sources9
Turni64 – 66Combined sources3
Helixi70 – 79Combined sources10
Helixi83 – 94Combined sources12
Turni96 – 98Combined sources3
Helixi99 – 101Combined sources3
Turni102 – 105Combined sources4
Helixi108 – 144Combined sources37
Turni145 – 147Combined sources3
Beta strandi149 – 154Combined sources6
Beta strandi157 – 163Combined sources7
Helixi164 – 188Combined sources25
Turni196 – 198Combined sources3
Helixi202 – 207Combined sources6
Turni208 – 210Combined sources3
Helixi212 – 225Combined sources14
Beta strandi236 – 238Combined sources3
Helixi242 – 270Combined sources29
Beta strandi273 – 275Combined sources3
Helixi295 – 308Combined sources14
Helixi311 – 319Combined sources9
Helixi327 – 329Combined sources3
Helixi330 – 357Combined sources28
Helixi362 – 384Combined sources23
Turni422 – 425Combined sources4
Turni427 – 429Combined sources3
Helixi430 – 438Combined sources9
Helixi440 – 443Combined sources4
Helixi447 – 457Combined sources11
Helixi459 – 463Combined sources5
Helixi464 – 466Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ21774.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 15Substrate binding; shared with neighboring subunitBy similarity2
Regioni81 – 83Substrate bindingBy similarity3
Regioni107 – 108Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
GeneTreeiENSGT00390000013486.
HOGENOMiHOG000033915.
InParanoidiQ21774.
KOiK01756.
OMAiWRKLWIA.
OrthoDBiEOG091G06S3.
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_016396353 – 370NIFEG…KKIVE → VSVLKITSSKDLVYKQTM in isoform b. CuratedAdd BLAST18
Alternative sequenceiVSP_016397371 – 478Missing in isoform b. CuratedAdd BLAST108

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YISX-ray2.40A1-478[»]
ProteinModelPortaliQ21774.
SMRiQ21774.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi37909. 2 interactors.
STRINGi6239.R06C7.5a.2.

Proteomic databases

EPDiQ21774.
PaxDbiQ21774.
PeptideAtlasiQ21774.
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.
OrthoDBiEOG091G06S3.
PhylomeDBiQ21774.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ21774.
PROiQ21774.

Gene expression databases

BgeeiWBGene00011064.

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...

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: November 30, 2016
This is version 139 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.