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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Staphylococcus aureus (strain MW2)
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 sitei95Substrate1
Active sitei141Proton donor/acceptorBy similarity1
Binding sitei212Substrate1
Binding sitei259Substrate1
Active sitei262Proton donor/acceptorBy similarity1
Binding sitei276Substrate1
Binding sitei301SubstrateBy similarity1
Binding sitei306SubstrateBy similarity1
Binding sitei310Substrate1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processPurine biosynthesis

Enzyme and pathway databases

BRENDAi4.3.2.2. 3352.
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:MW1849
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000418 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002599781 – 431Adenylosuccinate lyaseAdd BLAST431

Proteomic databases

PRIDEiQ7A0G9.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 13Combined sources6
Helixi16 – 36Combined sources21
Helixi42 – 51Combined sources10
Helixi56 – 66Combined sources11
Helixi69 – 80Combined sources12
Helixi83 – 87Combined sources5
Turni88 – 91Combined sources4
Helixi94 – 130Combined sources37
Turni131 – 133Combined sources3
Beta strandi135 – 140Combined sources6
Beta strandi143 – 149Combined sources7
Helixi150 – 175Combined sources26
Beta strandi176 – 178Combined sources3
Helixi192 – 202Combined sources11
Helixi217 – 244Combined sources28
Turni246 – 248Combined sources3
Beta strandi250 – 252Combined sources3
Beta strandi261 – 264Combined sources4
Helixi272 – 284Combined sources13
Helixi286 – 293Combined sources8
Helixi304 – 333Combined sources30
Helixi338 – 344Combined sources7
Turni345 – 350Combined sources6
Helixi351 – 353Combined sources3
Helixi354 – 362Combined sources9
Turni363 – 365Combined sources3
Turni368 – 375Combined sources8
Helixi376 – 384Combined sources9
Helixi389 – 393Combined sources5
Helixi405 – 407Combined sources3
Turni409 – 411Combined sources3
Helixi414 – 418Combined sources5
Helixi421 – 427Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X75X-ray2.50A1-431[»]
ProteinModelPortaliQ7A0G9.
SMRiQ7A0G9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7A0G9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 5Substrate binding2
Regioni67 – 69Substrate binding3

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.

Q7A0G9-1 [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
BA000033 Genomic DNA. Translation: BAB95714.1.
RefSeqiWP_000572878.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB95714; BAB95714; BAB95714.
KEGGisam:MW1849.

Similar proteinsi

Entry informationi

Entry nameiPUR8_STAAW
AccessioniPrimary (citable) accession number: Q7A0G9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 92 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

3D-structure, Complete proteome