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B2ICM9 (PURA_BEII9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:Bind_0262
OrganismBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]
Taxonomic identifier395963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeBeijerinckia

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceInferred 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 processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000089269

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding332 – 3343GTP By similarity
Nucleotide binding414 – 4163GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region300 – 3067Substrate binding By similarity

Sites

Active site131Proton acceptor By similarity
Active site411Proton donor By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity
Binding site1311IMP By similarity
Binding site1451IMP; shared with dimeric partner By similarity
Binding site2251IMP By similarity
Binding site2401IMP By similarity
Binding site3041IMP By similarity
Binding site3061GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2ICM9 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 44A913822C63E03F

FASTA43146,542
        10         20         30         40         50         60 
MANVVVVGAQ WGDEGKGKIV DWLSIEADIV VRFQGGHNAG HTLVIGNQVY KLALLPSGIV 

        70         80         90        100        110        120 
RLGKLSVIGN GVVVDPQHLV EEIAKLAAQG IEITPDNLKI AENVPLILGL HRELDAHRES 

       130        140        150        160        170        180 
STVEGVKIGT TKRGIGPAYE DKVGRRAIRL MDLAEPDTLD EKIVRLLAHH EPLRRGLGLE 

       190        200        210        220        230        240 
PISAGAIRAE LESLAPKILP FMDATWDLLE NARRAGKRIL FEGAQGALLD IDHGTYPFVT 

       250        260        270        280        290        300 
SSNTVAANAA TGSGLGPKAI GYVLGIAKAY TTRVGGGPFP TELLDETGQL IGDRGHEYGV 

       310        320        330        340        350        360 
NTGRRRRCGW FDAVLVRQTV KTCGIDGIAL TKLDILDGFK EIKVCVGYDL DGRRIDRLPA 

       370        380        390        400        410        420 
SQSAQARVKP IYETIDGWEG TTAGARSWAD LPAQAIKYVR RIEELIEAPV ALLSTSPERA 

       430 
DTILVHDPFR D 

« Hide

References

[1]"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. expand/collapse author list , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9039 / DSM 1715 / NCIB 8712.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001016 Genomic DNA. Translation: ACB93918.1.
RefSeqYP_001831407.1. NC_010581.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2ICM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6199228.
GenomeReviewsGene locus Bind_0262 in contig CP001016_GR.
KEGGbid:Bind_0262.
PATRIC21083095. VBIBeiInd21058_0506.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYDELMQV.
ProtClustDBCLSK2613283.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
KOK01939.
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
TIGRFAMsTIGR00184. PurA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_BEII9
AccessionPrimary (citable) accession number: B2ICM9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families