Reviewed, UniProtKB/Swiss-Prot Q6HAG9 (PURA_BACHK)

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:	BT9727_5148

Organism

Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]

Taxonomic identifier

180856 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	429 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 – 429	429	Adenylosuccinate synthetase HAMAP MF_00011		PRO_0000224254
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)
	Q6HAG9-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 0E44D5BA065649D5	FASTA	429	47,424
	10 20 30 40 50 60 MSSVVVVGTQ WGDEGKGKIT DFLSEHAEVV ARYQGGNNAG HTIVFGGVKY KLHLIPSGIF 70 80 90 100 110 120 YKEKICVIGN GLVVDPKALL EELKYLHDRG VSTDNLRVSN RAHVILPYHL KQDELEEASK 130 140 150 160 170 180 GDNKIGTTKK GIGPAYMDKA ARIGIRMADL LDREAFKEKL EQNLAQKNRL FEKMYDTEGF 190 200 210 220 230 240 SVDEIFEEYF EYGQQIAQYV CDTSVVLNDA LDNNHRVLFE GAQGVMLDID HGTYPFVTSS 250 260 270 280 290 300 NPIAGGVTVG TGVGPAKVTR VVGVCKAYTS RVGDGPFPTE LHDEIGHQIR EVGREYGTTT 310 320 330 340 350 360 GRPRRVGWFD SVVVRHARRV SGLTDLSLNS IDVLTGIPTL KICVAYKCDG KVIDEVPANL 370 380 390 400 410 420 NILAKCEPVY EELPGWTEDI TGVRSLDELP ENARKYVERV SELTGIQLSM FSVGPDRNQT NIVRNVYEA

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT63408.1.
RefSeq	YP_039457.1.
3D structure databases
SMR	Q6HAG9. Positions 2-429.
ModBase	Search...
Genome annotation databases
GeneID	2854099.
GenomeReviews	Gene locus BT9727_5148 in contig AE017355_GR.
KEGG	btk:BT9727_5148.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG658237.
OMA	IPVCVAY.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_5148-MONOMER.
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_BACHK

Accession

Primary (citable) accession number: Q6HAG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 45 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)