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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

N6-(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)DescriptionActionsGraphical viewLength
Binding sitei95SubstrateBy similarity1
Active sitei141Proton donor/acceptorBy similarity1
Binding sitei212SubstrateBy similarity1
Binding sitei259SubstrateBy similarity1
Active sitei262Proton donor/acceptorBy similarity1
Binding sitei276SubstrateBy similarity1
Binding sitei301SubstrateBy similarity1
Binding sitei306SubstrateBy similarity1
Binding sitei310SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processPurine 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:SA1724
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002599791 – 431Adenylosuccinate lyaseAdd BLAST431

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ7A4Q3
SMRiQ7A4Q3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 5Substrate bindingBy similarity2
Regioni67 – 69Substrate bindingBy similarity3

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000033912
KOiK01756
OMAiASSCEKI

Family and domain databases

Gene3Di1.10.275.10, 1 hit
InterProiView protein in InterPro
IPR019468 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
PfamiView protein in Pfam
PF10397 ADSL_C, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SMARTiView protein in SMART
SM00998 ADSL_C, 1 hit
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR00928 purB, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 1 hit

Sequencei

Sequence statusi: Complete.

Q7A4Q3-1 [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:July 5, 2004 - v1
Checksum:i493F79CBE814B9E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA Translation: BAB42994.1
PIRiC89979
RefSeqiWP_000572878.1, NC_002745.2

Genome annotation databases

EnsemblBacteriaiBAB42994; BAB42994; BAB42994
KEGGisau:SA1724

Similar proteinsi

Entry informationi

Entry nameiPUR8_STAAN
AccessioniPrimary (citable) accession number: Q7A4Q3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 93 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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