Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8FJC0 (PURA_BACP2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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
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:BPUM_3693
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length429 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 – 429429Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000057086

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding330 – 3323GTP By similarity
Nucleotide binding412 – 4143GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region298 – 3047Substrate 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 site1281IMP By similarity
Binding site1421IMP; shared with dimeric partner By similarity
Binding site2231IMP By similarity
Binding site2381IMP By similarity
Binding site3021IMP By similarity
Binding site3041GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FJC0 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 5E1E0F46545734A2

FASTA42947,597
        10         20         30         40         50         60 
MSSVVVVGTQ WGDEGKGKIT DFLSENAEVI ARYQGGNNAG HTIKFDGVTY KLHLIPSGIF 

        70         80         90        100        110        120 
YKEKTCVIGN GMVVDPKALV TELAYLHERN VSTDNLRISN RAHVILPYHL KLDEVEEERK 

       130        140        150        160        170        180 
GANKIGTTKK GIGPAYMDKA ARIGIRVADL LDREVFEEKL ARNLEEKNRL LEKMYEAEGF 

       190        200        210        220        230        240 
KIEDILDEYY EYGQQVKKYV VDTSVVLNDA LDEGRRVLFE GAQGVMLDID QGTYPFVTSS 

       250        260        270        280        290        300 
NPVAGGVTIG SGVGPTKIQH VVGVSKAYTT RVGDGPFPTE LHDEIGDQIR EVGREYGTTT 

       310        320        330        340        350        360 
GRPRRVGWFD SVVVRHARRV SGITDLSLNS IDVLTGIETL KICVAYKLNG EITEEFPASL 

       370        380        390        400        410        420 
NELAKCEPVY EEMPGWTEDI TGVKNLSELP ENARHYLERI SQLTGIPLSI FSVGPDRSQT 


NVVRSVYRP

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000813 Genomic DNA. Translation: ABV64337.1.
RefSeqYP_001488897.1. NC_009848.1.

3D structure databases

ProteinModelPortalA8FJC0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FJC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000063024; EBBACP00000061357; EBBACG00000063015.
GeneID5622991.
GenomeReviewsGene locus BPUM_3693 in contig CP000813_GR.
KEGGbpu:BPUM_3693.
PATRIC18971356. VBIBacPum16546_3743.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
GeneTreeEBGT00050000001253.
HOGENOMHBG658237.
OMADYVVRYQ.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycBPUM315750:BPUM_3693-MONOMER.

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_BACP2
AccessionPrimary (citable) accession number: A8FJC0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 30 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents