Reviewed, UniProtKB/Swiss-Prot Q7VWM1 (PURA_BORPE)

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:	BP2188

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	435 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. 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: 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_0000095151
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)
	Q7VWM1-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F35A4158E82013C2	FASTA	435	46,776
	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 SNLFALQQEG KNLLFEGAQG ALLDVDHGTY 250 260 270 280 290 300 PFVTSSNCVA GAASAGAGVG PQALQYVLGI TKAYTTRVGS GPFPTELVDE IGARLATIGK 310 320 330 340 350 360 EFGSVTGRPR RCGWLDGAAL KRSVRLNGIS GLCITKLDVL DGLETIQLGV GYRVNGEFRD 370 380 390 400 410 420 VLPYGAHAVA QAQAVLEELP GWTESTVGIT EYSKLPVNAR RYLERVAEVC GVPIDLVSTG 430 PDRNKTIVLR 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: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640417 Genomic DNA. Translation: CAE42466.1.
RefSeq	NP_880836.1.
3D structure databases
SMR	Q7VWM1. Positions 6-434.
ModBase	Search...
Genome annotation databases
GeneID	2666913.
KEGG	bpe:BP2188.
NMPDR	fig|257313.1.peg.1910.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG658237.
OMA	YVLGIIK.
PhylomeDB	Q7VWM1.
Enzyme and pathway databases
BioCyc	BPER257313:BP2188-MONOMER.
BRENDA	6.3.4.4. 21511.
Family and domain databases
HAMAP	MF_00011. Adenylosucc_synth. [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]
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_BORPE

Accession

Primary (citable) accession number: Q7VWM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 44 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)