Reviewed, UniProtKB/Swiss-Prot Q0VMF3 (PURA_ALCBS)

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:	ABO_2197

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	430 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 – 430	430	Adenylosuccinate synthetase HAMAP MF_00011		PRO_1000000771
Regions
	Nucleotide binding	13 – 19	7	GTP Potential
Sites
	Active site	141	1	By similarity
	Active site	148	1	By similarity
	Metal binding	14	1	Magnesium By similarity
	Metal binding	41	1	Magnesium; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VMF3-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 13D93C906D4FF4BA	FASTA	430	46,611
	10 20 30 40 50 60 MGKNVVILGT QWGDEGKGKI VDLLTDQASL VARFQGGHNA GHTLVIDGKK TVLHLIPSGI 70 80 90 100 110 120 LREDVQCLIG NGVVLSLEAL LKEIGGLEDQ GVPVRDRLRL SASCPLILPV HVALDQAREA 130 140 150 160 170 180 ARGNKKIGTT GRGIGPAYED KVARRGLRLG DVYQRELFAA KLGEVMDYHN FVLRSYYNAE 190 200 210 220 230 240 PVDFQKTLDD TLQLGEDVRS MVTDVTAVLH GARERGENIM FEGAQGTLLD IDHGTYPYVT 250 260 270 280 290 300 SSNTTAGGTA TGTGFGPLYL DYVLGITKAY TTRVGSGPFP TELFDENGRY LAEKGHEFGS 310 320 330 340 350 360 TTGRARRCGW FDAVALKRSI QINSITGLCL TKLDVLDGLE EINICVGYQD AAGNSLECAW 370 380 390 400 410 420 DADSYEEVKP VYESLPGWSE STLGVKSEDD LPPNAKAYLK RIEAITGAPI DIISTGPDRV 430 ETIIKRHPFS

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL17645.1.
RefSeq	YP_693917.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4211140.
GenomeReviews	Gene locus ABO_2197 in contig AM286690_GR.
KEGG	abo:ABO_2197.
NMPDR	fig|393595.12.peg.2197.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VMF3.
OMA	Q0VMF3. YVLGIIK.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_2197-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_ALCBS

Accession

Primary (citable) accession number: Q0VMF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 24 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)