Q72WW1 (PURA_BACC1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate synthetase
Short name=AMPSase
Short name=AdSS
EC=6.3.4.4

Alternative name(s):
IMP--aspartate ligase

Gene names

Name:	purA
Ordered Locus Names:	BCE_5617

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP By similarity. HAMAP MF_00011
Catalytic activity	GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP MF_00011
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00011
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011
Subunit structure	Homodimer By similarity. HAMAP MF_00011
Subcellular location	Cytoplasm By similarity HAMAP MF_00011.
Sequence similarities	Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylosuccinate synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 429	429	Adenylosuccinate synthetase HAMAP MF_00011		PRO_0000224250
Regions
	Nucleotide binding	12 – 18	7	GTP By similarity
	Nucleotide binding	40 – 42	3	GTP By similarity
	Nucleotide binding	330 – 332	3	GTP By similarity
	Nucleotide binding	412 – 414	3	GTP By similarity
	Region	13 – 16	4	IMP binding By similarity
	Region	38 – 41	4	IMP binding By similarity
	Region	298 – 304	7	Substrate binding By similarity
Sites
	Active site	13	1	Proton acceptor By similarity
	Active site	41	1	Proton donor By similarity
	Metal binding	13	1	Magnesium By similarity
	Metal binding	40	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	128	1	IMP By similarity
	Binding site	142	1	IMP; shared with dimeric partner By similarity
	Binding site	223	1	IMP By similarity
	Binding site	238	1	IMP By similarity
	Binding site	302	1	IMP By similarity
	Binding site	304	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72WW1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 0CC2C87E7AA1AE4B	FASTA	429	47,516
	10 20 30 40 50 60 MSSVVVVGTQ WGDEGKGKIT DFLSEHAEVV ARYQGGNNAG HTIVFGGVKY KLHLIPSGIF 70 80 90 100 110 120 YKEKICVIGN GLVVDPKALL EELKYLHDRG VSTDNLRVSN RAHVILPYHL KQDELEEASK 130 140 150 160 170 180 GDNKIGTTKK GIGPAYMDKA ARIGIRMADL LDREAFKEKL ERNLAQKNRL FEKMYDTEGF 190 200 210 220 230 240 SVEEIFEEYF EYGQQIAQYV CDTSVVLNDA LDNNHRVLFE GAQGVMLDID HGTYPFVTSS 250 260 270 280 290 300 NPIAGGVTVG TGVGPAKVTR VVGVCKAYTS RVGDGPFPTE LHDEIGHQIR EVGREYGTTT 310 320 330 340 350 360 GRPRRVGWFD SVVVRHARRV SGLTDLSLNS IDVLTGISTL KICVAYKYNG EVIDEVPANL 370 380 390 400 410 420 NILAKCEPVY EELPGWTEDI TGVRSLDELP ENARKYVERV SELTGIQLSM FSVGPDRNQT NIVRNVYEA

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017194 Genomic DNA. Translation: AAS44517.1.
RefSeq	NP_981909.1. NC_003909.8.
3D structure databases
ProteinModelPortal	Q72WW1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q72WW1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000029816; EBBACP00000029166; EBBACG00000029807.
GeneID	2750592.
GenomeReviews	Gene locus BCE_5617 in contig AE017194_GR.
KEGG	bca:BCE_5617.
NMPDR	fig|222523.1.peg.5581.
PATRIC	18859828. VBIBacCer118379_5379.
TIGR	BCE_5617.
Phylogenomic databases
eggNOG	COG0104.
GeneTree	EBGT00050000001253.
HOGENOM	HBG658237.
OMA	DYVVRYQ.
ProtClustDB	PRK01117.
Enzyme and pathway databases
BioCyc	BCER405917:BCE_5617-MONOMER.
Family and domain databases
HAMAP	MF_00011. Adenylosucc_synth. [Tree]
InterPro	IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view]
KO	K01939.
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
SMART	SM00788. Adenylsucc_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR00184. PurA. 1 hit.
PROSITE	PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PURA_BACC1

Accession

Primary (citable) accession number: Q72WW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program