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B6YR45 (PURA_AZOPC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 20. 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:CFPG_404
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

Protein attributes

Sequence length419 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 – 419419Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000089268

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding327 – 3293GTP By similarity
Nucleotide binding407 – 4093GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region295 – 3017Substrate 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 site2201IMP By similarity
Binding site2351IMP By similarity
Binding site2991IMP By similarity
Binding site3011GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6YR45 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: BEDC0F3054D83FBD

FASTA41946,614
        10         20         30         40         50         60 
MKVSVLLGLQ WGDEGKGKVV DVLTPKYDIV ARFQGGPNAG HTLLFADRKY VLCSIPSGVF 

        70         80         90        100        110        120 
QGKVNIIGNG VVLDPILFKA ETETLTSSCS NLVDKIYISR KAHLILPTHR LLDVAYETQK 

       130        140        150        160        170        180 
GNNKIGTTGK GIGPAYTDKV SRNGLRIGDI DYNFEEKYRY AIARHKELLH QMNFQYDLLP 

       190        200        210        220        230        240 
LEREWKKSIE VIKRFKRINS DNFINKALIG GRTVLAEGAQ GTMLDVDFGS YPFVTSSNTI 

       250        260        270        280        290        300 
CASACTGLGV APAKIGDVFG IFKAYCTRVG SGPFPTELSD EIGEKLRNIG NEYGSITKRP 

       310        320        330        340        350        360 
RRCGWIDLVA LRYAVMINGV TQLIMMKSDV LDTFDTVKAC IAYEVNGQKM EDFPFEIGSS 

       370        380        390        400        410 
VKPIYTELVG WKTNMTKIKS ENEFPKAFKD YLLFLEESLG VSIKIVSLGP DREQTIIRE

« Hide

References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP010656 Genomic DNA. Translation: BAG83667.1.
RefSeqYP_002309078.1. NC_011565.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB6YR45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7039407.
GenomeReviewsGene locus CFPG_404 in contig AP010656_GR.
KEGGaps:CFPG_404.
PATRIC31962556. VBICanAzo57536_0645.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMADYVVRYQ.
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_AZOPC
AccessionPrimary (citable) accession number: B6YR45
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: January 25, 2012
This is version 20 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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