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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
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)
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
Binding sitei95 – 951SubstrateBy similarity
Active sitei141 – 1411Proton donor/acceptorBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Binding sitei259 – 2591SubstrateBy similarity
Active sitei262 – 2621Proton donor/acceptorBy similarity
Binding sitei276 – 2761SubstrateBy similarity
Binding sitei301 – 3011SubstrateBy similarity
Binding sitei306 – 3061SubstrateBy similarity
Binding sitei310 – 3101SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1963-MONOMER.
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:SAV1908
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Adenylosuccinate lyasePRO_0000259977Add
BLAST

Proteomic databases

PaxDbiQ99SX9.

2D gel databases

World-2DPAGE0002:Q99SX9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi158878.SAV1908.

Structurei

3D structure databases

ProteinModelPortaliQ99SX9.
SMRiQ99SX9. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 52Substrate bindingBy similarity
Regioni67 – 693Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
PhylomeDBiQ99SX9.

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.

Q99SX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIERYSREEM SNIWTDQNRY EAWLEVEILA CEAWSELGHI PKADVQKIRQ
60 70 80 90 100
NAKVNVERAQ EIEQETRHDV VAFTRQVSET LGEERKWVHY GLTSTDVVDT
110 120 130 140 150
ALSFVIKQAN DIIEKDLERF IDVLAEKAKN YKYTLMMGRT HGVHAEPTTF
160 170 180 190 200
GVKMALWYTE MQRNLQRFKQ VREEIEVGKM SGAVGTFANI PPEIESYVCK
210 220 230 240 250
HLGIGTAPVS TQTLQRDRHA YYIATLALIA TSLEKFAVEI RNLQKTETRE
260 270 280 290 300
VEEAFAKGQK GSSAMPHKRN PIGSENITGI SRVIRGYITT AYENVPLWHE
310 320 330 340 350
RDISHSSAER IMLPDVTIAL DYALNRFTNI VDRLTVFEDN MRNNIDKTFG
360 370 380 390 400
LIFSQRVLLA LINKGMVREE AYDKVQPKAM ISWETKTPFR ELIEQDESIT
410 420 430
SVLTKEELDE CFDPKHHLNQ VDTIFERAGL A
Length:431
Mass (Da):49,603
Last modified:June 1, 2001 - v1
Checksum:i493F79CBE814B9E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58070.1.
RefSeqiWP_000572878.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58070; BAB58070; SAV1908.
KEGGisav:SAV1908.
PATRICi19564670. VBIStaAur52173_1975.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58070.1.
RefSeqiWP_000572878.1. NC_002758.2.

3D structure databases

ProteinModelPortaliQ99SX9.
SMRiQ99SX9. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1908.

2D gel databases

World-2DPAGE0002:Q99SX9.

Proteomic databases

PaxDbiQ99SX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB58070; BAB58070; SAV1908.
KEGGisav:SAV1908.
PATRICi19564670. VBIStaAur52173_1975.

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
PhylomeDBiQ99SX9.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciSAUR158878:GJJ5-1963-MONOMER.

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_STAAM
AccessioniPrimary (citable) accession number: Q99SX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
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

Complete 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.