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A7NEW1 (PURA_FRATF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 39. 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:FTA_2039
OrganismFrancisella tularensis subsp. holarctica (strain FTNF002-00 / FTA) [Complete proteome] [HAMAP]
Taxonomic identifier458234 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella ›

Protein attributes

Sequence length428 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 committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_00011

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule 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-Rule 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_process'de novo' AMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 428428Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_1000000823

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding331 – 3333GTP By similarity
Nucleotide binding410 – 4123GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region299 – 3057Substrate 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 site1291IMP By similarity
Binding site1431IMP; shared with dimeric partner By similarity
Binding site2241IMP By similarity
Binding site2391IMP By similarity
Binding site3031IMP By similarity
Binding site3051GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7NEW1 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 721299C7F0031FB4

FASTA42846,880
        10         20         30         40         50         60 
MSNIVIVGAQ WGDEGKGKIA DTLAEKADLV VRYQGGNNAG HTLVVNGKKT FLHLIPSGVL 

        70         80         90        100        110        120 
HQHTKCVIGH GVVLDPVALD EEITRLQAKG IAISAENLFV SESCTIITSY HKLLDAVRES 

       130        140        150        160        170        180 
NTSEKIGTTG KGIGPAYEDK VSRKGIKFKH LFDKDLLRSR LAISLAEKET LFRDLYKVEY 

       190        200        210        220        230        240 
PTLEQEFDKL FALGQKLKQY AADTFSIIDQ AIAAGKNVVY EGAQGVLLDV DYGTYPFVTS 

       250        260        270        280        290        300 
SNTSVAGVYS GATTAGHGLD HVIGITKAYT TRVGEGPFPT ELFDDVGKFI QHKGGEIGVT 

       310        320        330        340        350        360 
TGRIRRCGWL DLPLLKYSAK CSNLTSIALT KVDVLSDMDT LKVCIGYKYE GKEIYCAYPG 

       370        380        390        400        410        420 
IDLYKVEPIL VEMEPFSIDE TVTKDNMPAA LKTYLKTIEN HVGIPISSLA YGPSREQILF 


FEDYFKKG

« Hide

References

[1]"Complete genome sequence of Francisella tularensis subspecies holarctica FTNF002-00."
Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J., Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W., Lion C., Dempsey M.P.
PLoS ONE 4:E7041-E7041(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FTNF002-00 / FTA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000803 Genomic DNA. Translation: ABU62514.1.
RefSeqYP_001429470.1. NC_009749.1.

3D structure databases

ProteinModelPortalA7NEW1.
ModBaseSearch...

Protein-protein interaction databases

STRING119857.FTL_1930.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU62514; ABU62514; FTA_2039.
GeneID5523199.
KEGGfta:FTA_2039.
PATRIC17949556. VBIFraTul129798_2118.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMADYVVRYQ.
ProtClustDBPRK13784.

Enzyme and pathway databases

BioCycFTUL458234:GH31-1798-MONOMER.
UniPathwayUPA00075; UER00335.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 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_FRATF
AccessionPrimary (citable) accession number: A7NEW1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: May 1, 2013
This is version 39 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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