Reviewed, UniProtKB/Swiss-Prot Q5PAA8 (PURA_ANAMM)

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:	AM856

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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 – 426	426	Adenylosuccinate synthetase HAMAP MF_00011		PRO_0000224248
Regions
	Nucleotide binding	12 – 18	7	GTP Potential
Sites
	Active site	141	1	By similarity
	Active site	148	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)
	Q5PAA8-1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 7BCF0C7B4939586B	FASTA	426	46,284
	10 20 30 40 50 60 MASIVVVGLQ WGDEGKGKIV DWLSVSADAV VRFQGGNNAG HTVVADGRVY KLSLLPTSVL 70 80 90 100 110 120 RQNKLSMIGS GVALDPYALV REVDSLKDSG IFLDPDSLCL SESCPLVLSV HRDADSIMEE 130 140 150 160 170 180 MRGNESIGTT CMGIGPCYED KVGRRAIRLC DLLDETSLYD KVLCLLSYHN LLRRATNRRE 190 200 210 220 230 240 VTPHEIMDEL TQIAPKVLPF MKPVPEIIVS LIKQGKTVLF EGAQGALLDI DHGTYPYVTS 250 260 270 280 290 300 SNTVAGYVRV GCGVGALGDM RVLGLAKAYT TRVGNGPFAT EQTGTVGDAM FERGREVGTV 310 320 330 340 350 360 TNRVRRCGWF DAVSVRQAAL SSGASEMVIT KLDVLDTIDE IKVCTKYRCG EESYDYLPAA 370 380 390 400 410 420 SHIQNRLEPV YETLPGWRTS TLGAVSRSDL PENAVSYISR LEELVGVPVS LVSTGPERNH IVPMNP

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV86772.1. Different initiation.
RefSeq	YP_154027.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PAA8.
Genome annotation databases
GeneID	3171522.
GenomeReviews	Gene locus AM856 in contig CP000030_GR.
KEGG	ama:AM856.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5PAA8.
OMA	IPVCVAY.
Enzyme and pathway databases
BioCyc	AMAR234826:AM856-MON.
Family and domain databases
HAMAP	MF_00011. [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]
ProDom	PD001188. Asucc_synthtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_ANAMM

Accession

Primary (citable) accession number: Q5PAA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	November 3, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)