Q39PN9 (PURA2_BURS3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate synthetase 2
Short name=AMPSase 2
Short name=AdSS 2
EC=6.3.4.4

Alternative name(s):
IMP--aspartate ligase 2

Gene names

Name:	purA2
Ordered Locus Names:	Bcep18194_C6526

Organism

Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]

Taxonomic identifier

269483 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	432 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 – 432	432	Adenylosuccinate synthetase 2 HAMAP MF_00011		PRO_0000224265
Regions
	Nucleotide binding	12 – 18	7	GTP By similarity
	Nucleotide binding	40 – 42	3	GTP By similarity
	Nucleotide binding	329 – 331	3	GTP By similarity
	Nucleotide binding	411 – 413	3	GTP By similarity
	Region	13 – 16	4	IMP binding By similarity
	Region	38 – 41	4	IMP binding By similarity
	Region	297 – 303	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	222	1	IMP By similarity
	Binding site	237	1	IMP By similarity
	Binding site	301	1	IMP By similarity
	Binding site	303	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q39PN9 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: E8B1AC0AA0B3D792	FASTA	432	45,920
	10 20 30 40 50 60 MPNVVVVGAQ WGDEGKGRVV DWLAAQADLV ARYNGGHNAG HTLVVGGKTY KLALLPSGVV 70 80 90 100 110 120 RGKRGVIGNG VALDPEALLA EIGRMAELGL SVTPDNLSIA ENATLVLPIH RAIDQAQERL 130 140 150 160 170 180 RREPIGTTLR GIGPAYEDKV GRRGLRVGDL AEPGRLAAKL DVLVDHHNAW FRGLGLDEYS 190 200 210 220 230 240 RDAMLATLVD LAPRILPFVR PVWADLNDAT DRGERILFEG SQAVMLDIDW GTYPFVTSSG 250 260 270 280 290 300 TVASAAAAGT GLGASKLGHV LGVTKAYATR VGGGPFLTEL SDATGETLRA RGQEFGVNTG 310 320 330 340 350 360 RPRRCGWLDA AQLRQAVRIS GIDSLALTKL DVLDGFESIE LCVGYEFDGA RVDHLPASLD 370 380 390 400 410 420 AQSRAKPVYE RFDGWRGTVK GVRERAALPR AAQDFIARVE AVAGAPVSMI TTGAERDDTI 430 VLRNPFDAAA GA

References

[1]

"Complete sequence of chromosome 3 of Burkholderia sp. 383." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 383.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000150 Genomic DNA. Translation: ABB05577.1.
RefSeq	YP_366221.1. NC_007509.1.
3D structure databases
ProteinModelPortal	Q39PN9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q39PN9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3733882.
GenomeReviews	Gene locus Bcep18194_C6526 in contig CP000150_GR.
KEGG	bur:Bcep18194_C6526.
NMPDR	fig|269483.3.peg.3735.
PATRIC	19281078. VBIBurSp120713_0003.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0104.
HOGENOM	HBG658237.
OMA	PIHRAID.
ProtClustDB	CLSK941367.
Enzyme and pathway databases
BioCyc	BSP36773:BCEP18194_C6526-MONOMER.
Family and domain databases
HAMAP	MF_00011. Adenylosucc_synth. Divergent sequence. [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

PURA2_BURS3

Accession

Primary (citable) accession number: Q39PN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	November 22, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program