Q4L7M3 (PUR8_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate lyase
Short name=ASL
EC=4.3.2.2

Alternative name(s):
Adenylosuccinase
Short name=ASase

Gene names

Name:	purB
Ordered Locus Names:	SH1043

Organism

Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]

Taxonomic identifier

279808 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	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.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
Sequence similarities	Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine ribonucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Adenylosuccinate lyase		PRO_0000259984
Sites
	Active site	68	1	Proton donor By similarity
	Active site	141	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4L7M3 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: 88C7A78DF1E97747	FASTA	431	49,894
	10 20 30 40 50 60 MIDRYSREEM ANIWTDQNRY EAWLEVEILA CEAWSELGHI PKEDVKKIRQ NAKVDVKRAQ 70 80 90 100 110 120 EIEQETRHDV VAFTRQVSET LGDERKWVHY GLTSTDVVDT ALSYVIKQAN EIIEKDIERF 130 140 150 160 170 180 IKVLEEKAKN YKYTLMMGRT HGVHAEPTTF GVKMALWYTE MKRNLKRFKE VRKEIEVGKM 190 200 210 220 230 240 SGAVGTFANI PPEIEQYVCD HLGIDTASVS TQTLQRDRHA YYIATLALVA TSLEKFAVEI 250 260 270 280 290 300 RNLQKTETRE VEEAFAKGQK GSSAMPHKRN PIGSENITGI SRVIRGYITT AYENVPLWHE 310 320 330 340 350 360 RDISHSSAER IMLPDVTIAL DYALNRFTNI VDRLTVFEDN MRNNIDKTFG LIFSQRVLLA 370 380 390 400 410 420 LINKGMVREE AYDRVQPKAM ESWETKTPFR QLIEKDESIT NVLSKEELDE CFNPEHHLNQ 430 VDTIFKRAGL E

References

[1]

"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC1435.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006716 Genomic DNA. Translation: BAE04352.1.
RefSeq	YP_252958.1. NC_007168.1.
3D structure databases
ProteinModelPortal	Q4L7M3.
SMR	Q4L7M3. Positions 2-430.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4L7M3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000044124; EBSTAP00000042575; EBSTAG00000044122.
GeneID	3481954.
GenomeReviews	Gene locus SH1043 in contig AP006716_GR.
KEGG	sha:SH1043.
NMPDR	fig|279808.3.peg.1757.
PATRIC	19618135. VBIStaHae67511_1029.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0015.
GeneTree	EBGT00050000024473.
HOGENOM	HBG499008.
OMA	KEVKHDV.
PhylomeDB	Q4L7M3.
ProtClustDB	PRK08937.
Enzyme and pathway databases
BioCyc	SHAE279808:SH1043-MONOMER.
Family and domain databases
InterPro	IPR019468. AdenyloSucc_lyase_C. IPR003031. D_crystallin. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR022761. Lyase1_N. IPR004769. Pur_lyase. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KO	K01756.
PANTHER	PTHR11444:SF2. PTHR11444:SF2. 1 hit.
Pfam	PF10397. ADSL_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
SMART	SM00998. ADSL_C. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00928. PurB. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR8_STAHJ

Accession

Primary (citable) accession number: Q4L7M3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2006
Last sequence update:	August 2, 2005
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program