Q814H1 (PURA_BACCR) 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:	BC_5468

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [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 Reference 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_0000095144
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)
	Q814H1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D7B87F76C3FDDA58	FASTA	429	47,569
	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 ERNLVEKNRL FEKMYDTEGF 190 200 210 220 230 240 TVEEIFEEYF 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 IDVLTGIPTL KICVAYKYNG EVIDEVPANL 370 380 390 400 410 420 NILAKCEPVY EELPGWEEDI TGVKSLDELP ENARKYVERV SELTGIQISM FSVGPDRNQT NIVRNVYEA

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP12324.1.
RefSeq	NP_835123.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q814H1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q814H1.
Proteomic databases
PRIDE	Q814H1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000032570; EBBACP00000031776; EBBACG00000032561.
GeneID	1207808.
GenomeReviews	Gene locus BC_5468 in contig AE016877_GR.
KEGG	bce:BC5468.
PATRIC	32607158. VBIBacCer54481_5646.
Phylogenomic databases
eggNOG	COG0104.
GeneTree	EBGT00050000001253.
HOGENOM	HBG658237.
OMA	DYVVRYQ.
PhylomeDB	Q814H1.
ProtClustDB	PRK01117.
Enzyme and pathway databases
BioCyc	BCER226900:BC_5468-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_BACCR

Accession

Primary (citable) accession number: Q814H1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program