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Reviewed, UniProtKB/Swiss-Prot Q8A6N4 (PURA_BACTN)

Last modified November 3, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
    AdSS
    AMPSase
Gene names
Name: purA
Ordered Locus Names: BT_1843
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. 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.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: HAMAP

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095147

Regions

Nucleotide binding12 – 187GTP Potential

Sites

Active site1401 By similarity
Active site1471 By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A6N4-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1569243D88FB2FDB

FASTA42346,789
        10         20         30         40         50         60 
MKVDVLLGLQ WGDEGKGKVV DVLTPKYDVV ARFQGGPNAG HTLEFEGQKY VLRSIPSGIF 

        70         80         90        100        110        120 
QGDKVNIIGN GVVLDPALFK AEAEALEASG HPLKERLHIS KKAHLILPTH RILDAAYEAA 

       130        140        150        160        170        180 
KGDAKVGTTG KGIGPTYTDK VSRNGVRVGD ILHNFEQKYG AAKARHEQIL KSLNYEYDLT 

       190        200        210        220        230        240 
ELEKAWMEGI EYLKQFHFVD SEHEVNNYLK DGKSVLCEGA QGTMLDIDFG SYPFVTSSNT 

       250        260        270        280        290        300 
VCAGACTGLG VAPNRIGEVF GIFKAYCTRV GAGPFPTELF DETGDKMCTL GHEFGSVTGR 

       310        320        330        340        350        360 
KRRCGWIDLV ALKYSVMING VTKLIMMKSD VLDTFDTIKA CVAYKVDGEE IDYFPYDITE 

       370        380        390        400        410        420 
GVEPVYAELP GWKTDMTKMQ SEDEFPEEFN AYLTFLEEQL GVEIKIVSVG PDRAQTIERY 


TEE 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO76950.1.
RefSeqNP_810756.1.

3D structure databases

HSSPHSSP built from PDB template 1ADE based on UniProtKB P12283.
ModBaseSearch...

Genome annotation databases

GeneID1075166.
GenomeReviewsGene locus BT_1843 in contig AE015928_GR.
KEGGbth:BT_1843.
NMPDRfig|226186.1.peg.1843.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8A6N4.
OMAIPVCVAY.

Enzyme and pathway databases

BioCycBTHE226186:BT_1843-MON.
BRENDA6.3.4.4. 21018.

Family and domain databases

HAMAPMF_00011.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
ProDomPD001188. Asucc_synthtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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_BACTN
AccessionPrimary (citable) accession number: Q8A6N4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents