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A1W588 (PURA_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. 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:Ajs_1181
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length458 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 – 458458Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000321791

Regions

Nucleotide binding17 – 237GTP By similarity
Nucleotide binding45 – 473GTP By similarity
Nucleotide binding358 – 3603GTP By similarity
Nucleotide binding440 – 4423GTP By similarity
Region18 – 214IMP binding By similarity
Region43 – 464IMP binding By similarity
Region326 – 3327Substrate binding By similarity

Sites

Active site181Proton acceptor By similarity
Active site461Proton donor By similarity
Metal binding181Magnesium By similarity
Metal binding451Magnesium; via carbonyl oxygen By similarity
Binding site1371IMP By similarity
Binding site1511IMP; shared with dimeric partner By similarity
Binding site2471IMP By similarity
Binding site2621IMP By similarity
Binding site3301IMP By similarity
Binding site3321GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W588 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: ED10C6FCD2345D5F

FASTA45849,378
        10         20         30         40         50         60 
MKASKGRNVV VVGTQWGDEG KGKLVDWLTE SAQGVVRFQG GHNAGHTLVI NGVKTALHLI 

        70         80         90        100        110        120 
PSGIMRPGVK CYIGNGVVLS AGKLFEEIEG LEKAGVEVRS RLRVSEACPL ILPFHAALDV 

       130        140        150        160        170        180 
AREAAREHGG AEKIGTTGRG IGPAYEDKIA RRALRVQDLK YPERFAAKLR ELLALHNHVL 

       190        200        210        220        230        240 
STFLGSANFQ FGDALKPYIT GGQVQFEPVF EEAMRHAEML KPMMADVSRE LNEAHAAGAN 

       250        260        270        280        290        300 
LLFEGAQGTL LDVDHGTYPY VTSSNCVAGN AAAGSGVGPG HLHYILGITK AYCTRVGGGP 

       310        320        330        340        350        360 
FPTELDWETP GTPGYHMSTV GAEKGVTTGR SRRCGWFDAA LLKRSAQVNG LSGLCITKLD 

       370        380        390        400        410        420 
VLDGLRELSL CVGYELDGER IDLLPMGAEE IARCVPIYEN IAGWTESTVG VTHYENLPSN 

       430        440        450 
ARRYLERIEQ VTGVPIAMIS TSPDRDHTIL MRHPYAAD 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000539 Genomic DNA. Translation: ABM41413.1.
RefSeqYP_985489.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1W588.
SMRA1W588. Positions 6-457.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1W588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4672451.
GenomeReviewsGene locus Ajs_1181 in contig CP000539_GR.
KEGGajs:Ajs_1181.
PATRIC20687670. VBIAciSp27161_1386.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBA1W588.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycASP232721:AJS_1181-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_ACISJ
AccessionPrimary (citable) accession number: A1W588
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 37 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