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Protein

Adenylosuccinate lyase

Gene

ADSL

Organism
Gallus gallus (Chicken)
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), 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. Multifunctional protein ADE2 (AIRC)
  2. Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), 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 sitei160 – 1601Proton donor/acceptorBy similarity
Binding sitei242 – 2421SubstrateBy similarity
Active sitei290 – 2901Proton donor/acceptorBy similarity
Binding sitei304 – 3041Substrate; shared with neighboring subunitBy similarity
Binding sitei330 – 3301SubstrateBy similarity
Binding sitei335 – 3351SubstrateBy similarity
Binding sitei339 – 3391SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiR-GGA-419140. De novo synthesis of IMP.
R-GGA-421203. De novo synthesis of AMP.
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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Adenylosuccinate lyasePRO_0000137895Add
BLAST

Proteomic databases

PaxDbiP21265.
PRIDEiP21265.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9031.ENSGALP00000037110.

Structurei

3D structure databases

ProteinModelPortaliP21265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 222Substrate binding; shared with neighboring subunitBy similarity
Regioni86 – 883Substrate bindingBy similarity
Regioni112 – 1132Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP21265.
KOiK01756.
PhylomeDBiP21265.

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.

P21265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPCAEEDP LARYRSPLVS RYASAEMGFN FSERKKFGTW RRLWLYLAQA
60 70 80 90 100
EKSLGLPITD EQIKEMEANL DNIDFKMAAE EEKKLRHDVM AHVHTFAHCC
110 120 130 140 150
PKAAAIIHLG ATSCYVGDNT DLIVLRDGFN LLLPKLARVI SRLADFAETH
160 170 180 190 200
ADLPTLGFTH YQPAQLTTVG KRCCLWIQDL CMDLQNLERA RDDLRFRGVK
210 220 230 240 250
GTTGTQASFL QLFEGDHSKV EELDRLVTAK AGFKRSYMVT GQTYSRKVDI
260 270 280 290 300
EVLSVLASLG ASVHKICTDI RLLANLKEIE EPFEKDQIGS SAMPYKRNPM
310 320 330 340 350
RSERCCSLAR HLMTLVLDPL QTASVQWFER TLDDSANRRV CLAEAFLTAD
360 370 380 390 400
IILSTLQNIS EGLVVYPKVI DRRIRQELPF MATENIIMAM VKAGGNRQDC
410 420 430 440 450
HEKIRVLSQQ AAAVVKQEGG DNDFIARVRA DPYFSPIHEH LDSLLDPSSF
460 470 480
TGRAPQQVAK FLKEEVRPAL IPYQSMMGGK IELTL
Length:485
Mass (Da):54,653
Last modified:September 2, 2008 - v2
Checksum:iFCBADBF37E812CF0
GO

Sequence cautioni

The sequence AAA48574 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAT76521 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571A → G in ABU24460 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY665559 Genomic DNA. Translation: AAT76521.1. Different initiation.
EU049886 mRNA. Translation: ABU24460.1.
M37901 mRNA. Translation: AAA48574.1. Different initiation.
PIRiA35291.
RefSeqiNP_990860.1. NM_205529.1.
UniGeneiGga.2721.

Genome annotation databases

GeneIDi396540.
KEGGigga:396540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY665559 Genomic DNA. Translation: AAT76521.1. Different initiation.
EU049886 mRNA. Translation: ABU24460.1.
M37901 mRNA. Translation: AAA48574.1. Different initiation.
PIRiA35291.
RefSeqiNP_990860.1. NM_205529.1.
UniGeneiGga.2721.

3D structure databases

ProteinModelPortaliP21265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000037110.

Proteomic databases

PaxDbiP21265.
PRIDEiP21265.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396540.
KEGGigga:396540.

Organism-specific databases

CTDi158.

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
HOGENOMiHOG000033915.
HOVERGENiHBG000214.
InParanoidiP21265.
KOiK01756.
PhylomeDBiP21265.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
ReactomeiR-GGA-419140. De novo synthesis of IMP.
R-GGA-421203. De novo synthesis of AMP.

Miscellaneous databases

PROiP21265.

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...

Entry informationi

Entry nameiPUR8_CHICK
AccessioniPrimary (citable) accession number: P21265
Secondary accession number(s): A7UEA6, Q6BCQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: September 2, 2008
Last modified: June 8, 2016
This is version 112 of the entry and version 2 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.