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Reviewed, UniProtKB/Swiss-Prot Q3MBG1 (PURA_ANAVT)

Last modified November 3, 2009. Version 31. 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: Ava_2053
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length447 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 – 447447Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000000775

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
Q3MBG1-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: C45B513FAEB7AC80

FASTA44749,140
        10         20         30         40         50         60 
MANVIVIGAQ WGDEGKGKIT DLLSRSADVV VRYQGGVNAG HTIVVKGQTF KLHLIPSGIL 

        70         80         90        100        110        120 
YPDTECMIGC GTVIDPQVLI KELDQLESLN ISTKNLLISE TAHVTMPYHR LIDKASEERR 

       130        140        150        160        170        180 
GSHKIGTTGR GIGPTYADKS ERTGIRVLDL MDPAALRDQL AWTINNKNLI LEKLYNLPPL 

       190        200        210        220        230        240 
DTEEVVKEYL GYAERLRPHV VDTSLKIYDA IQRRRNILFE GAQGTLLDLD HGTYPYVTSS 

       250        260        270        280        290        300 
NPVAGGACVG TGLGPTMIDR VIGVSKAYTT RVGEGPFPTE LDGELGELLC DRGAEFGTTT 

       310        320        330        340        350        360 
GRKRRCGWFD AVIGRYAVRI NGMDCMAITK LDVLDELEEI QVCIAYEIDG DRCDHFPTSA 

       370        380        390        400        410        420 
RQFARCRPIY KTLPGWQVPT SECRTLEDLP QQALDYLKFL AELMEVPIAI VSLGASRDQT 

       430        440 
IIVEDPIHGP KRALLHPDGT PASLLSA 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000117 Genomic DNA. Translation: ABA21675.1.
RefSeqYP_322570.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MBG1.

Genome annotation databases

GeneID3680702.
GenomeReviewsGene locus Ava_2053 in contig CP000117_GR.
KEGGava:Ava_2053.
NMPDRfig|240292.3.peg.3133.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3MBG1.
OMAIPVCVAY.

Enzyme and pathway databases

BioCycAVAR240292:AVA_2053-MON.

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_ANAVT
AccessionPrimary (citable) accession number: Q3MBG1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2005
Last modified: November 3, 2009
This is version 31 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