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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 1711Proton donor/acceptor1 Publication
Binding sitei247 – 2471Substrate
Active sitei295 – 2951Proton donor/acceptor1 Publication
Binding sitei309 – 3091Substrate
Binding sitei335 – 3351Substrate
Binding sitei340 – 3401SubstrateBy similarity

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi171 – 1711H → A or N: Reduces catalytic activity about 500-fold. 1 Publication
Mutagenesisi295 – 2951S → A: Reduces catalytic activity about 1000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Adenylosuccinate lyasePRO_0000137878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941N6-acetyllysine1 Publication
Modified residuei366 – 3661N6-acetyllysine1 Publication

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 interactions.
DIPiDIP-10608N.
IntActiP0AB89. 11 interactions.
MINTiMINT-1253735.
STRINGi511145.b1131.

Structurei

Secondary structure

1
456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 73Combined sources
Turni11 – 166Combined sources
Helixi17 – 193Combined sources
Helixi21 – 255Combined sources
Helixi29 – 4921Combined sources
Helixi61 – 7212Combined sources
Helixi76 – 8914Combined sources
Helixi92 – 10413Combined sources
Helixi108 – 1114Combined sources
Helixi112 – 1165Combined sources
Turni117 – 1204Combined sources
Helixi123 – 14119Combined sources
Helixi143 – 16018Combined sources
Turni161 – 1633Combined sources
Beta strandi165 – 1706Combined sources
Beta strandi173 – 1797Combined sources
Helixi180 – 20021Combined sources
Helixi215 – 2206Combined sources
Helixi226 – 23611Combined sources
Beta strandi246 – 2483Combined sources
Helixi252 – 28029Combined sources
Beta strandi283 – 2864Combined sources
Helixi305 – 32723Combined sources
Helixi338 – 3425Combined sources
Helixi343 – 3453Combined sources
Helixi346 – 36621Combined sources
Beta strandi367 – 3693Combined sources
Helixi371 – 3788Combined sources
Helixi382 – 3854Combined sources
Helixi386 – 39510Combined sources
Helixi401 – 4077Combined sources
Helixi416 – 4249Combined sources
Beta strandi426 – 4283Combined sources
Helixi430 – 4378Combined sources
Helixi441 – 4433Combined sources
Helixi448 – 4547Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AB89.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 162Substrate binding
Regioni90 – 923Substrate binding
Regioni122 – 1232Substrate binding
Regioni301 – 3033Substrate binding
Regioni340 – 3445Substrate binding

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451P → A in AAA92731 (PubMed:1729205).Curated
Sequence conflicti154 – 1541I → L in AAA92731 (PubMed:1729205).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2PTQX-ray2.00A/B1-456[»]
2PTRX-ray1.85A/B1-456[»]
2PTSX-ray2.00A1-456[»]
ProteinModelPortaliP0AB89.
SMRiP0AB89. Positions 2-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262847. 274 interactions.
DIPiDIP-10608N.
IntActiP0AB89. 11 interactions.
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: September 7, 2016
This is version 100 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.