A9IK82 (PURA_BORPD) 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:	Bpet2031

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	431 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 – 431	431	Adenylosuccinate synthetase HAMAP MF_00011		PRO_1000089272
Regions
	Nucleotide binding	13 – 19	7	GTP By similarity
	Nucleotide binding	41 – 43	3	GTP By similarity
	Nucleotide binding	332 – 334	3	GTP By similarity
	Nucleotide binding	414 – 416	3	GTP By similarity
	Region	14 – 17	4	IMP binding By similarity
	Region	39 – 42	4	IMP binding By similarity
	Region	300 – 306	7	Substrate binding By similarity
Sites
	Active site	14	1	Proton acceptor By similarity
	Active site	42	1	Proton donor By similarity
	Metal binding	14	1	Magnesium By similarity
	Metal binding	41	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	130	1	IMP By similarity
	Binding site	144	1	IMP; shared with dimeric partner By similarity
	Binding site	225	1	IMP By similarity
	Binding site	240	1	IMP By similarity
	Binding site	304	1	IMP By similarity
	Binding site	306	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9IK82 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: CAA4C6BCBE2502FE	FASTA	431	46,089
	10 20 30 40 50 60 MSKNVVVIGT QWGDEGKGKI VDWLAESVQG VVRFQGGHNA GHTLWINGKK TILRLIPSGI 70 80 90 100 110 120 MHPGVTCFIG NGVVLSPEAL LKEIEELEAA GLDVRSRLQI SEICPLILPY HIAVDQAREA 130 140 150 160 170 180 RKGEGKIGTT GRGIGPAYED KIARRALRVQ DLFNPALFDE KLAELLDYHN FVLTQYLGAP 190 200 210 220 230 240 AVSAAQVRDQ AMALAPAIAP MVKDVSSNLY AMQQAGQRLL FEGAQGALLD VDHGTYPFVT 250 260 270 280 290 300 SSNCLAGAAS AGAGVGPQSL DYVLGITKAY TTRVGSGPFP TELVDEIGTR LATIGKEFGS 310 320 330 340 350 360 VTGRPRRCGW FDGAALKRSV RLNGITGLCI TKLDVLDGLE SIQLGVGYRV NGEFRDVLPY 370 380 390 400 410 420 GAHAVAQAEA VLEELPGWSE STVGITEYAK LPAAARRYLE RVAEVCGVPI DLVSTGPDRN 430 ETIVLRHPLK G

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP42371.1.
RefSeq	YP_001630640.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9IK82.
SMR	A9IK82. Positions 2-430.
ModBase	Search...
Protein-protein interaction databases
STRING	A9IK82.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5817347.
GenomeReviews	Gene locus Bpet2031 in contig AM902716_GR.
KEGG	bpt:Bpet2031.
PATRIC	21165525. VBIBorPet31633_2027.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG658237.
OMA	DYVQPMK.
ProtClustDB	PRK01117.
Enzyme and pathway databases
BioCyc	BPET94624:BPET2031-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_BORPD

Accession

Primary (citable) accession number: A9IK82

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program