A7ZAP4 (PURA_BACA2) 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:	RBAM_037450

Organism

Bacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]

Taxonomic identifier

326423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	430 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 – 430	430	Adenylosuccinate synthetase HAMAP MF_00011		PRO_1000000779
Regions
	Nucleotide binding	12 – 18	7	GTP By similarity
	Nucleotide binding	40 – 42	3	GTP By similarity
	Nucleotide binding	330 – 332	3	GTP By similarity
	Nucleotide binding	412 – 414	3	GTP By similarity
	Region	13 – 16	4	IMP binding By similarity
	Region	38 – 41	4	IMP binding By similarity
	Region	298 – 304	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	223	1	IMP By similarity
	Binding site	238	1	IMP By similarity
	Binding site	302	1	IMP By similarity
	Binding site	304	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZAP4 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: CDE72E2402941ABF	FASTA	430	47,700
	10 20 30 40 50 60 MSSVVVVGTQ WGDEGKGKIT DFLSENAEVI ARYQGGNNAG HTIKFDGVTY KLHLIPSGIF 70 80 90 100 110 120 YKEKACVIGN GMVVDPKALI TELAYLHERN VSTDNLRISN RAHVILPYHL KLDEVEEERK 130 140 150 160 170 180 GANKIGTTKK GIGPAYMDKA ARIGIRIADL LDRDVFAEKL ERNLEEKNRL LEKMYETEGF 190 200 210 220 230 240 KIEDILDEYY EYGQQIKKYV CDTSVVLNDA LDEGRRVLFE GAQGVMLDID QGTYPFVTSS 250 260 270 280 290 300 NPVAGGVTIG SGVGPTKIQH VVGVSKAYTT RVGDGPFPTE LKDEIGDQIR EVGREYGTTT 310 320 330 340 350 360 GRPRRVGWFD SVVVRHARRV SGITDLSLNS IDVLTGIETL KICVAYRYKG EVIEEFPASL 370 380 390 400 410 420 KALAECEPVY EEMPGWTEDI TGAKTLSDLP ENARHYLERV SQLTGIPLSI FSVGPDRSQT 430 NVIRSVYRAN

References

[1]

"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42." Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R. Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FZB42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000560 Genomic DNA. Translation: ABS76070.1.
RefSeq	YP_001423301.1. NC_009725.1.
3D structure databases
ProteinModelPortal	A7ZAP4.
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZAP4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000007588; EBBACP00000007466; EBBACG00000007580.
GeneID	5460682.
GenomeReviews	Gene locus RBAM_037450 in contig CP000560_GR.
KEGG	bay:RBAM_037450.
PATRIC	18752716. VBIBacAmy31356_3800.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0104.
GeneTree	EBGT00050000001253.
HOGENOM	HBG658237.
OMA	DYVVRYQ.
ProtClustDB	PRK01117.
Enzyme and pathway databases
BioCyc	BAMY326423:RBAM_037450-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_BACA2

Accession

Primary (citable) accession number: A7ZAP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 23, 2007
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program