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Q39FS0 (PURA1_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase 1
Short name=AMPSase 1
Short name=AdSS 1
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase 1
Gene names
Name:purA1
Ordered Locus Names:Bcep18194_A5102
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length448 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 – 448448Adenylosuccinate synthetase 1 HAMAP MF_00011
PRO_0000224264

Regions

Nucleotide binding22 – 287GTP By similarity
Nucleotide binding50 – 523GTP By similarity
Nucleotide binding349 – 3513GTP By similarity
Nucleotide binding431 – 4333GTP By similarity
Region23 – 264IMP binding By similarity
Region48 – 514IMP binding By similarity
Region317 – 3237Substrate binding By similarity

Sites

Active site231Proton acceptor By similarity
Active site511Proton donor By similarity
Metal binding231Magnesium By similarity
Metal binding501Magnesium; via carbonyl oxygen By similarity
Binding site1391IMP By similarity
Binding site1531IMP; shared with dimeric partner By similarity
Binding site2341IMP By similarity
Binding site2491IMP By similarity
Binding site3211IMP By similarity
Binding site3231GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39FS0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 59ABC05C2C92CDBC

FASTA44848,133
        10         20         30         40         50         60 
MSASAVNVTP GRNVVVVGTQ WGDEGKGKIV DWLTDHAQGV VRFQGGHNAG HTLIIGGKKT 

        70         80         90        100        110        120 
ILRLIPSGIM REGVACYIGN GVVLSPEALF KEIGELEEAG VNVRDRLFIS EATTLILPYH 

       130        140        150        160        170        180 
IAIDQAREAR KGAGKIGTTG RGIGPAYEDK VGRRALRVQD LFDAKTFADR LRENLDFHNF 

       190        200        210        220        230        240 
VLTQYLGGAA VDFQATLDTM LGYADRLKPM VADVSRRLYD ANNAGQNLLF EGAQGTLLDI 

       250        260        270        280        290        300 
DHGTYPFVTS SNCVAGAASA GAGVGPQKLN YILGITKAYC TRVGSGPFPS ELYDADNPQR 

       310        320        330        340        350        360 
QDQVGVTLAN VGKEFGSVTG RPRRTGWLDA AALRRSIQIN GVSGLCMTKL DVLDGLDEVK 

       370        380        390        400        410        420 
LCVGYKIDGK DADILPRGAA DVARCEPVYE TFAGWKESTV GIKTWEALPA NAQAYLTRVQ 

       430        440 
EVAGVPVDMV STGPDRDETI LLRHPFKV

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000151 Genomic DNA. Translation: ABB08696.1.
RefSeqYP_369340.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39FS0.
SMRQ39FS0. Positions 11-447.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39FS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3750310.
GenomeReviewsGene locus Bcep18194_A5102 in contig CP000151_GR.
KEGGbur:Bcep18194_A5102.
NMPDRfig|269483.3.peg.6177.
PATRIC19287593. VBIBurSp120713_3201.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMAYVLGIIK.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A5102-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 namePURA1_BURS3
AccessionPrimary (citable) accession number: Q39FS0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 46 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

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