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Reviewed, UniProtKB/Swiss-Prot A6TXB3 (PURA_ALKMQ)

Last modified November 3, 2009. Version 14. 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: Amet_4765
OrganismAlkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]
Taxonomic identifier293826 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length427 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 – 427427Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000057085

Regions

Nucleotide binding12 – 187GTP Potential

Sites

Active site1391 By similarity
Active site1461 By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A6TXB3-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: A7EB132D6D68C0D4

FASTA42747,970
        10         20         30         40         50         60 
MPSIVIVGAQ WGDEGKGKII DYLAQEADVV IRAQGGNNAG HTVMVEDKKY SFHLLPSGVL 

        70         80         90        100        110        120 
FEDKLNIIGN GVVFDPEGFL QEIEVLKKEG INTSNIKIDE RVHVIFPYHK RIDQLEEEAR 

       130        140        150        160        170        180 
GEAQIGTTKK GIGPCYMDKI QRSGIRLGEM IDEEDFKDRL YKQVDDKNKI IEKIYEAEGF 

       190        200        210        220        230        240 
EKEAMYETYL KYAREIKKYV TDTTILAHEA LKAKKKVLFE GAQGTLLDID LGTYPYVTSS 

       250        260        270        280        290        300 
HPTAGGFPIG AGIGPNQIEQ VLGIVKAYTT RVGSGTFPTE LDNEVGDKIR IKGNEFGTTT 

       310        320        330        340        350        360 
GRPRRCGWFD GVMVRYTTRI NGLTAMSLML LDVLSGFDTL KICTGYELEG EMVAHFPANI 

       370        380        390        400        410        420 
KTLGKCKPIY EELPGWEEDI TNMKTYEELP ENAKKYIERI ESYVGVPIKM ISVGPKRNQT 


IIRERLF 

« Hide

References

[1]"Complete sequence of Alkaliphilus metalliredigens QYMF."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000724 Genomic DNA. Translation: ABR50831.1.
RefSeqYP_001322490.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6TXB3.

Genome annotation databases

GeneID5314930.
GenomeReviewsGene locus Amet_4765 in contig CP000724_GR.
KEGGamt:Amet_4765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIPVCVAY.

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_ALKMQ
AccessionPrimary (citable) accession number: A6TXB3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: November 3, 2009
This is version 14 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