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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N(6)-(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

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:ASL-MONOMER.
ECOL316407:JW1117-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
Complete GO annotation...

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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4262847. 274 interactors.
DIPiDIP-10608N.
IntActiP0AB89. 11 interactors.
MINTiMINT-1253735.
STRINGi511145.b1131.

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.
InterProiIPR024083. 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.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

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.
PATRICi32117511. VBIEscCol129921_1178.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi4262847. 274 interactors.
DIPiDIP-10608N.
IntActiP0AB89. 11 interactors.
MINTiMINT-1253735.
STRINGi511145.b1131.

Proteomic databases

EPDiP0AB89.
PaxDbiP0AB89.
PRIDEiP0AB89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74215; AAC74215; b1131.
BAA35953; BAA35953; BAA35953.
GeneIDi945695.
KEGGiecj:JW1117.
eco:b1131.
PATRICi32117511. VBIEscCol129921_1178.

Organism-specific databases

EchoBASEiEB1290.
EcoGeneiEG11314. purB.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
InParanoidiP0AB89.
KOiK01756.
OMAiTQVNPCD.
PhylomeDBiP0AB89.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciEcoCyc:ASL-MONOMER.
ECOL316407:JW1117-MONOMER.
MetaCyc:ASL-MONOMER.
BRENDAi4.3.2.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AB89.
PROiP0AB89.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR024083. 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.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPUR8_ECOLI
AccessioniPrimary (citable) accession number: P0AB89
Secondary accession number(s): P25739
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.