Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenylosuccinate lyase

Gene

purB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP.1 Publication
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.1 Publication

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 (purA)
  2. Adenylosuccinate lyase (purB)
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. Phosphoribosylaminoimidazole-succinocarboxamide synthase (purC)
  2. Adenylosuccinate lyase (purB)
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 sitei171Proton donor/acceptor1 Publication1
Binding sitei247Substrate1
Active sitei295Proton donor/acceptor1 Publication1
Binding sitei309Substrate1
Binding sitei335Substrate1
Binding sitei340SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processPurine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:ASL-MONOMER
MetaCyc:ASL-MONOMER
BRENDAi4.3.2.2 2026
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:purB
Ordered Locus Names:b1131, JW1117
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11314 purB

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi171H → A or N: Reduces catalytic activity about 500-fold. 1 Publication1
Mutagenesisi295S → A: Reduces catalytic activity about 1000-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001378781 – 456Adenylosuccinate lyaseAdd BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei94N6-acetyllysine1 Publication1
Modified residuei366N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0AB89
PaxDbiP0AB89
PRIDEiP0AB89

PTM databases

iPTMnetiP0AB89

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
aceEP0AFG82EBI-556534,EBI-542683

Protein-protein interaction databases

BioGridi4262847, 280 interactors
DIPiDIP-10608N
IntActiP0AB89, 11 interactors
STRINGi316385.ECDH10B_1203

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 7Combined sources3
Turni11 – 16Combined sources6
Helixi17 – 19Combined sources3
Helixi21 – 25Combined sources5
Helixi29 – 49Combined sources21
Helixi61 – 72Combined sources12
Helixi76 – 89Combined sources14
Helixi92 – 104Combined sources13
Helixi108 – 111Combined sources4
Helixi112 – 116Combined sources5
Turni117 – 120Combined sources4
Helixi123 – 141Combined sources19
Helixi143 – 160Combined sources18
Turni161 – 163Combined sources3
Beta strandi165 – 170Combined sources6
Beta strandi173 – 179Combined sources7
Helixi180 – 200Combined sources21
Helixi215 – 220Combined sources6
Helixi226 – 236Combined sources11
Beta strandi246 – 248Combined sources3
Helixi252 – 280Combined sources29
Beta strandi283 – 286Combined sources4
Helixi305 – 327Combined sources23
Helixi338 – 342Combined sources5
Helixi343 – 345Combined sources3
Helixi346 – 366Combined sources21
Beta strandi367 – 369Combined sources3
Helixi371 – 378Combined sources8
Helixi382 – 385Combined sources4
Helixi386 – 395Combined sources10
Helixi401 – 407Combined sources7
Helixi416 – 424Combined sources9
Beta strandi426 – 428Combined sources3
Helixi430 – 437Combined sources8
Helixi441 – 443Combined sources3
Helixi448 – 454Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PTQX-ray2.00A/B1-456[»]
2PTRX-ray1.85A/B1-456[»]
2PTSX-ray2.00A1-456[»]
ProteinModelPortaliP0AB89
SMRiP0AB89
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB89

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni15 – 16Substrate binding2
Regioni90 – 92Substrate binding3
Regioni122 – 123Substrate binding2
Regioni301 – 303Substrate binding3
Regioni340 – 344Substrate binding5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QTF Bacteria
COG0015 LUCA
HOGENOMiHOG000252916
InParanoidiP0AB89
KOiK01756
OMAiTQVNPCD
PhylomeDBiP0AB89

Family and domain databases

Gene3Di1.10.275.10, 1 hit
InterProiView protein in InterPro
IPR024083 Fumarase/histidase_N
IPR020557 Fumarate_lyase_CS
IPR000362 Fumarate_lyase_fam
IPR022761 Fumarate_lyase_N
IPR008948 L-Aspartase-like
IPR004769 Pur_lyase
IPR013539 PurB_C
PfamiView protein in Pfam
PF08328 ASL_C, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR00928 purB, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 1 hit

Sequencei

Sequence statusi: Complete.

P0AB89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSSLTAVS PVDGRYGDKV SALRGIFSEY GLLKFRVQVE VRWLQKLAAH
60 70 80 90 100
AAIKEVPAFA ADAIGYLDAI VASFSEEDAA RIKTIERTTN HDVKAVEYFL
110 120 130 140 150
KEKVAEIPEL HAVSEFIHFA CTSEDINNLS HALMLKTARD EVILPYWRQL
160 170 180 190 200
IDGIKDLAVQ YRDIPLLSRT HGQPATPSTI GKEMANVAYR MERQYRQLNQ
210 220 230 240 250
VEILGKINGA VGNYNAHIAA YPEVDWHQFS EEFVTSLGIQ WNPYTTQIEP
260 270 280 290 300
HDYIAELFDC VARFNTILID FDRDVWGYIA LNHFKQKTIA GEIGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGLSNAV LQHLASKLPV SRWQRDLTDS TVLRNLGVGI
360 370 380 390 400
GYALIAYQST LKGVSKLEVN RDHLLDELDH NWEVLAEPIQ TVMRRYGIEK
410 420 430 440 450
PYEKLKELTR GKRVDAEGMK QFIDGLALPE EEKARLKAMT PANYIGRAIT

MVDELK
Length:456
Mass (Da):51,543
Last modified:November 8, 2005 - v1
Checksum:i8D1F4546B66795BC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145P → A in AAA92731 (PubMed:1729205).Curated1
Sequence conflicti154I → L in AAA92731 (PubMed:1729205).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74924 Genomic DNA Translation: AAA92731.1
X59307 Genomic DNA Translation: CAA41996.1
U00096 Genomic DNA Translation: AAC74215.1
AP009048 Genomic DNA Translation: BAA35953.1
PIRiS19212
RefSeqiNP_415649.1, NC_000913.3
WP_000423742.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74215; AAC74215; b1131
BAA35953; BAA35953; BAA35953
GeneIDi945695
KEGGiecj:JW1117
eco:b1131
PATRICifig|1411691.4.peg.1135

Similar proteinsi

Entry informationi

Entry nameiPUR8_ECOLI
AccessioniPrimary (citable) accession number: P0AB89
Secondary accession number(s): P25739
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: March 28, 2018
This is version 111 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health