Reviewed, UniProtKB/Swiss-Prot B3DNT3 (PURA_BIFLD)

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
Ordered Locus Names:	BLD_1347

Organism

Bifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]

Taxonomic identifier

205913 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	428 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 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: 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 – 428	428	Adenylosuccinate synthetase HAMAP MF_00011		PRO_1000089270
Regions
	Nucleotide binding	12 – 18	7	GTP Potential
Sites
	Active site	139	1	By similarity
	Active site	146	1	By similarity
	Metal binding	13	1	Magnesium By similarity
	Metal binding	40	1	Magnesium; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	B3DNT3-1 [UniParc]. Last modified July 22, 2008. Version 1. Checksum: A9800204F2C85BC3	FASTA	428	46,469
	10 20 30 40 50 60 MPGIVLIGAQ WGDEGKGKAT DLIGTKVDYV ARFNGGNNAG HSVVVGDESY ALHLLPSGII 70 80 90 100 110 120 NPNLTPVIGN GVVVDPEVLF EEIDGLESRG IDCSHLKVSE AAHIIAPYHR TLDKVTERFL 130 140 150 160 170 180 GKHKIGTTGR GIGPAYADKI NRVGIRVHDL FNADHLHDKV EASLHQKNQM LVKLYNRRPI 190 200 210 220 230 240 DVDQTTEELL KLGERLKPYV ANTGLILNKA LDEGKTVLFE GAQATMLDVD HGTYPFVTSS 250 260 270 280 290 300 NPTAGGACTG TGVGPTKITR VIGVSKAYVT RVGEGPFPTE LLDESGEWLR QQGHEFGVTT 310 320 330 340 350 360 GRPRRCGWFD AVVNRYASQV NGLTDIVLTK LDVLTGLKEI PICVAYDVDG ERHDDMPTDQ 370 380 390 400 410 420 AAFAAAKPIY ETMPGWDEDI SDCHSFDELP ATCQAYVKRL EELSGCRISA IGTGPQRDHV IQINSLVD

References

[1]

"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth." Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J. BMC Genomics 9:247-247(2008) [PubMed: 18505588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000605 Genomic DNA. Translation: ACD98792.1.
RefSeq	YP_001955290.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6363174.
GenomeReviews	Gene locus BLD_1347 in contig CP000605_GR.
KEGG	blj:BLD_1347.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG658237.
OMA	IPVCVAY.
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_BIFLD

Accession

Primary (citable) accession number: B3DNT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	July 22, 2008
Last modified:	February 9, 2010
This is version 14 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)