Q7NS98 (PURA2_CHRVO) 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:	CV_3528

Organism

Chromobacterium violaceum [Complete proteome] [HAMAP]

Taxonomic identifier

536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

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 2 HAMAP MF_00011		PRO_0000095166
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)
	Q7NS98 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 373EE33F255E64BB	FASTA	431	46,638
	10 20 30 40 50 60 MSKNVVVIGT QWGDEGKGKI VDWLTDHARA VVRFQGGHNA GHTLWVNGKK TVVRLVPSGI 70 80 90 100 110 120 LRPDVECFIG NGVVLSPEAL LKEIDELEAA GVNASARLKI AEGCPLILPY HIALDQAREA 130 140 150 160 170 180 AKGDAKIGTT GRGIGPCYED KVARRALKVI DLFDPARFET KLKENVDYYN FLLTNLFKAE 190 200 210 220 230 240 PVSYEAILAD TMKMAERIKP MVADVSRTLY DLDKAGTPIL FEGAQGTLLD IDHGTYPYVT 250 260 270 280 290 300 SSNCVAGAAA PGAGVPPQML NYVLGIVKGY ATRVGSGPFP TEQENEIGAF LAKRGNEFGS 310 320 330 340 350 360 VTGRPRRCGW FDAAALKRSI QINGVSGLCV MKLDVMDGLE EIKLCTGYML DGQKVDILPF 370 380 390 400 410 420 GSDAVTKCEP VYETLPGWTG TTVGVKRWED LPANAQAYLK RIEEVCGAPV DIVSTGPDRE 430 ETIVLRHPFG L

References

[1]

"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G. Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016825 Genomic DNA. Translation: AAQ61190.1.
RefSeq	NP_903198.1. NC_005085.1.
3D structure databases
ProteinModelPortal	Q7NS98.
SMR	Q7NS98. Positions 4-429.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2547652.
GenomeReviews	Gene locus CV_3528 in contig AE016825_GR.
KEGG	cvi:CV_3528.
NMPDR	fig|243365.1.peg.3528.
PATRIC	21441869. VBIChrVio67196_3454.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG658237.
OMA	YVLGIIK.
PhylomeDB	Q7NS98.
ProtClustDB	PRK01117.
Enzyme and pathway databases
BioCyc	CVIO243365:CV_3528-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_CHRVO

Accession

Primary (citable) accession number: Q7NS98

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	December 15, 2003
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program