Reviewed, UniProtKB/Swiss-Prot Q7W6Q7 (PURA_BORPA)

Names and origin

Protein names

Recommended name:
    Adenylosuccinate synthetase
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
    AdSS
    AMPSase

Gene names

Name:	purA
Synonyms:	adeK
Ordered Locus Names:	BPP2844

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays an important role in the de novo pathway of purine nucleotide biosynthesis. 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.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: HAMAP adenylosuccinate synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 435	435	Adenylosuccinate synthetase HAMAP MF_00011		PRO_0000095150
Regions
	Nucleotide binding	17 – 23	7	GTP Potential
Sites
	Active site	145	1	By similarity
	Active site	152	1	By similarity
	Metal binding	18	1	Magnesium By similarity
	Metal binding	45	1	Magnesium; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W6Q7-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 424649350B48423A	FASTA	435	46,869
	10 20 30 40 50 60 MIRKMSKNVV VIGTQWGDEG KGKIVDWLAE SVQGVVRFQG GHNAGHTLWI NGKKTILRLI 70 80 90 100 110 120 PSGIMHDGVT CFIGNGVVLS PEALLREIEE LEAAGLDVRS RLQVSEICTL ILPYHVAVDK 130 140 150 160 170 180 AREARKGEGK IGTTGRGIGP AYEDKVARRA LRVQDLFNPA LFDEKLAEVL DYHNFVLTQY 190 200 210 220 230 240 LGAEPVSANE VRDQAMALAP ALAPMVRDVS SNLFVLQQEG KNLLFEGAQG ALLDVDHGTY 250 260 270 280 290 300 PFVTSSNCVA GAASAGAGVG PQALQYVLGI TKAYTTRVGS GPFPTELVDE IGTRLATIGK 310 320 330 340 350 360 EFGSVTGRPR RCGWFDGAAL KRSVRLNGIS GLCITKLDVL DGLETIQLGV GYRVNGEFRD 370 380 390 400 410 420 VLPYGAHAVA QAQAVLEELP GWTESTVGIT EYSKLPVNAR RYLERVAEVC GVPIDLVSTG 430 PDRNETIVLR HPFKG

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640431 Genomic DNA. Translation: CAE38136.1.
RefSeq	NP_885044.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1667787.
GenomeReviews	Gene locus BPP2844 in contig BX470249_GR.
KEGG	bpa:BPP2844.
NMPDR	fig|257311.1.peg.2678.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7W6Q7.
OMA	YVLGIIK.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP2844-MON.
BRENDA	6.3.4.4. 263123.
Family and domain databases
HAMAP	MF_00011. [Tree]
InterPro	IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view]
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
ProDom	PD001188. Asucc_synthtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_BORPA

Accession

Primary (citable) accession number: Q7W6Q7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)