NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ng.2007.38; PubMed=18037886 [NCBI, ExPASy, EBI, Israel, Japan]
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors.";
Nat. Genet. 39:1469-1476(2007).

Comments

FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis (By similarity).
CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + N⁶-(1,2-dicarboxyethyl)-AMP.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the adenylosuccinate synthetase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AM260525; CAK01015.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001609010.1; -.

3D structure databases

ModBase

A9IQ57.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004019;	Molecular function: adenylosuccinate synthase activity (inferred from electronic annotation from HAMAP).
GO:0005525;	Molecular function: GTP binding (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0006164;	Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00011; -; 1.
PBIL [Tree]

InterPro

IPR001114; AdlSucc_Synth.
Graphical view of domain structure.

PANTHER

PTHR11846; Asucc_synthtase; 1.

ProDom

PD001188; Asucc_synthtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00788; Adenylsucc_synt; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00184; purA; 1.

PROSITE

PS01266; ADENYLOSUCCIN_SYN_1; 1.
PS00513; ADENYLOSUCCIN_SYN_2; 1.

Genome annotation databases

GeneID

5829648; -.

GenomeReviews

AM260525_GR; BT0567.

CMR

A9IQ57; BT0567.

Other

ProtoNet

A9IQ57.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 429`	`429`	`Adenylosuccinate synthetase.`	`PRO_1000073937`
`NP_BIND`	`12 18`	`7`	`GTP (Potential).`
`ACT_SITE`	`140 140`		`By similarity.`
`ACT_SITE`	`147 147`		`By similarity.`
`METAL`	`13 13`		`Magnesium (By similarity).`
`METAL`	`40 40`		`Magnesium; via carbonyl oxygen (By similarity).`

Sequence information

Length: 429 AA [This is the length of the unprocessed precursor]

Molecular weight: 47190 Da [This is the MW of the unprocessed precursor]

CRC64: 007509CECE4632D3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANVVVVGTQ WGDEGKGKIV DWLSERADIV VRYQGGHNAG HTLVIDGVSY KLSLLPSGLV 

        70         80         90        100        110        120 
RGKLSIIGNG VVVDPHHFVA ELKKLCDQGV KITPEILRIA ENAPLILSLH RDLDAIRESG 

       130        140        150        160        170        180 
LSGLKIGTTK RGIGPAYEDK VGRRAIRVMD LAEKDTLMAK IERLLRHHNA LRRGMGVAEI 

       190        200        210        220        230        240 
DSQALYDELM QVADKILPFM DCTWRLLDEG YREGKHILFE GAQGALLDND FGTYPYVTSS 

       250        260        270        280        290        300 
NTVAGQACTG SGMGPGVIHY VLGIAKAYTT RVGEGPFPTE QINDIGEFLG TRGHEFGVVT 

       310        320        330        340        350        360 
GRKRRCGWFD AVLVRQMVAI CGVQGIALTK LDVLDGLDEI KICIGYELDG RKIDYLPSSM 

       370        380        390        400        410        420 
GAQARVKPIY ETLEGWKAKT AHTLRWEDLP VQAVKYIRYI EELINTKVAL LSTSPEREDT 


ILITDPFAN

A9IQ57 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools