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Q46ZJ3 (PURA1_CUPPJ) 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:Reut_A2076
OrganismCupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length446 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 – 446446Adenylosuccinate synthetase 1 HAMAP MF_00011
PRO_0000224312

Regions

Nucleotide binding20 – 267GTP By similarity
Nucleotide binding48 – 503GTP By similarity
Nucleotide binding347 – 3493GTP By similarity
Nucleotide binding429 – 4313GTP By similarity
Region21 – 244IMP binding By similarity
Region46 – 494IMP binding By similarity
Region315 – 3217Substrate binding By similarity

Sites

Active site211Proton acceptor By similarity
Active site491Proton donor By similarity
Metal binding211Magnesium By similarity
Metal binding481Magnesium; via carbonyl oxygen By similarity
Binding site1371IMP By similarity
Binding site1511IMP; shared with dimeric partner By similarity
Binding site2321IMP By similarity
Binding site2471IMP By similarity
Binding site3191IMP By similarity
Binding site3211GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46ZJ3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: D7469D952A757324

FASTA44647,981
        10         20         30         40         50         60 
MSASAVGQGR NVVVIGTQWG DEGKGKIVDW LTDHAKGVVR FQGGHNAGHT LIIGGKKTIL 

        70         80         90        100        110        120 
RLIPSGIMRE GTVCYIGNGV VLSPEALFRE IEELETAGLE VQKRLRISEA ATLILPYHVA 

       130        140        150        160        170        180 
IDKAREARRG AAKIGTTGRG IGPAYEDKVA RRALRVQDLF DPQQFAERLR ENLDFHNFML 

       190        200        210        220        230        240 
TQYLGAEAVD YQQTLDDALA FAPRLAPMVA DVSAELYAVN AAGGNLMFEG AQGTLLDVDH 

       250        260        270        280        290        300 
GTYPFVTSSN CVAGAAAAGA GVGPGRLSYI LGITKAYCTR VGAGPFPSEL YDNDNPARQD 

       310        320        330        340        350        360 
QVGVRLANVG KEFGSVTGRP RRTGWLDAAA LKRSVQINGV SGLCLTKLDV LDGLESIKLC 

       370        380        390        400        410        420 
VGYTLDGKTV DILPRGSDAV ARCEPVYEEF PGWNESTFGV KAWDALPEAA RVYLKRVEEV 

       430        440 
VGIPIDMIST GPDRDETILL RHPYLA

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000090 Genomic DNA. Translation: AAZ61440.1.
RefSeqYP_296284.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ46ZJ3.
SMRQ46ZJ3. Positions 9-446.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ46ZJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3611744.
GenomeReviewsGene locus Reut_A2076 in contig CP000090_GR.
KEGGreu:Reut_A2076.
NMPDRfig|264198.3.peg.2762.
PATRIC20229727. VBIRalEut24049_2719.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMASRCQGGN.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycREUT264198:REUT_A2076-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_CUPPJ
AccessionPrimary (citable) accession number: Q46ZJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 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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