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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 (purA)
  2. Adenylosuccinate lyase (purB), Adenylosuccinate lyase (PA3517)
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), Adenylosuccinate lyase (PA3517)
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/acceptorBy similarity
Binding sitei248 – 2481SubstrateBy similarity
Active sitei296 – 2961Proton donor/acceptorBy similarity
Binding sitei310 – 3101SubstrateBy similarity
Binding sitei336 – 3361SubstrateBy similarity
Binding sitei341 – 3411SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

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:PA2629
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA2629.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Adenylosuccinate lyasePRO_0000287829Add
BLAST

Proteomic databases

PaxDbiQ9I0K9.
PRIDEiQ9I0K9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi208964.PA2629.

Structurei

3D structure databases

ProteinModelPortaliQ9I0K9.
SMRiQ9I0K9. Positions 2-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 162Substrate bindingBy similarity
Regioni90 – 923Substrate bindingBy similarity
Regioni122 – 1232Substrate bindingBy similarity
Regioni302 – 3043Substrate bindingBy similarity
Regioni341 – 3455Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
InParanoidiQ9I0K9.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.
PhylomeDBiQ9I0K9.

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.

Q9I0K9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLSSLTAVS PVDGRYAGKT SSLRPIFSEY GLIRFRVMVE VRWLQRLAAH
60 70 80 90 100
AGIPEVAPFS AEANALLDSL ASDFQLEHAE RIKEIERTTN HDVKAVEYLL
110 120 130 140 150
KEQAAKLPEL AAVSEFIHFA CTSEDINNLS HALMLREGRD SVLLPLMRQI
160 170 180 190 200
AEAIRELAVK LADVPMLSRT HGQPASPTTL GKELANVVYR LERQIKQVAG
210 220 230 240 250
IELLGKINGA VGNYNAHLSA YPEVDWEANA RQFIEGDLGL TFNPYTTQIE
260 270 280 290 300
PHDYIAELFD AIARFNTILI DFDRDVWGYI SLGYFKQKTV AGEIGSSTMP
310 320 330 340 350
HKVNPIDFEN SEGNLGIANA LFQHLASKLP ISRWQRDLTD STVLRNLGVG
360 370 380 390 400
IAHSIIAYEA SLKGIGKLEL NAQRIAEDLD ACWEVLAEPV QTVMRRYGVE
410 420 430 440 450
NPYEKLKELT RGKGISAEAL QTFIEELAIP AEAKVELKKL TPAGYVGNAA

AQAKRI
Length:456
Mass (Da):50,501
Last modified:March 1, 2001 - v1
Checksum:i08648476573C398F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06017.1.
PIRiF83317.
RefSeqiNP_251319.1. NC_002516.2.
WP_003113371.1. NZ_ASJY01000431.1.

Genome annotation databases

EnsemblBacteriaiAAG06017; AAG06017; PA2629.
GeneIDi882336.
KEGGipae:PA2629.
PATRICi19839751. VBIPseAer58763_2751.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06017.1.
PIRiF83317.
RefSeqiNP_251319.1. NC_002516.2.
WP_003113371.1. NZ_ASJY01000431.1.

3D structure databases

ProteinModelPortaliQ9I0K9.
SMRiQ9I0K9. Positions 2-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA2629.

Proteomic databases

PaxDbiQ9I0K9.
PRIDEiQ9I0K9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06017; AAG06017; PA2629.
GeneIDi882336.
KEGGipae:PA2629.
PATRICi19839751. VBIPseAer58763_2751.

Organism-specific databases

PseudoCAPiPA2629.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
InParanoidiQ9I0K9.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.
PhylomeDBiQ9I0K9.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiPUR8_PSEAE
AccessioniPrimary (citable) accession number: Q9I0K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: February 17, 2016
This is version 97 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

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.