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A7HDA9 (PURA_ANADF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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
Short name=AMPSase
Short name=AdSS
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase
Gene names
Name:purA
Ordered Locus Names:Anae109_2504
OrganismAnaeromyxobacter sp. (strain Fw109-5) [Complete proteome] [HAMAP]
Taxonomic identifier404589 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

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_1000000774

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 site1301IMP By similarity
Binding site1441IMP; 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
A7HDA9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: F3874DD987AAA924

FASTA43146,656
        10         20         30         40         50         60 
MPNVVVVGAQ WGDEGKGKIV DLLTEHADVV VRFQGGNNAG HTLVVNGEKT VLHLIPAGIL 

        70         80         90        100        110        120 
HPGKSCVIGN GVVFDPEVFV MEVDRLKSRN ALADDSQLVV SLDAHVIMPW HKAIDIAREQ 

       130        140        150        160        170        180 
AMGAGKIGTT GRGIGPTYED KVARRGLRIR DLLDAARLER KVKERLPAAR EELSRLGATP 

       190        200        210        220        230        240 
ELDEAAIVAR YSELGRRVAR YAADVSLWLH RALQNGKQLL FEGAQGTMLD VDHGTYPFVT 

       250        260        270        280        290        300 
SSNTVAGNAV VGCGLGPTAV DYVLGISKAY STRVGGGPYP SELKDETGER LRKIGGEFGA 

       310        320        330        340        350        360 
TTGRPRRTGW LDALALRYAA RVNGLHGIAM TKLDVLAGFE TVKIAVGYRV DGKVLDEMPS 

       370        380        390        400        410        420 
DPELLERAEA VYEELPGWTE KLEDLRSWDD LPPRARAYVK RVEQLVGVPV VGLSVGADRG 

       430 
QTILLENPFR A

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. Fw109-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Fields M., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fw109-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000769 Genomic DNA. Translation: ABS26705.1.
RefSeqYP_001379689.1. NC_009675.1.

3D structure databases

ProteinModelPortalA7HDA9.
SMRA7HDA9. Positions 2-431.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7HDA9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5377286.
GenomeReviewsGene locus Anae109_2504 in contig CP000769_GR.
KEGGafw:Anae109_2504.
NMPDRfig|404589.4.peg.2167.
PATRIC20930317. VBIAnaSp113478_2623.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMAYVLGIIK.
ProtClustDBPRK01117.

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_ANADF
AccessionPrimary (citable) accession number: A7HDA9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 28 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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