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Reviewed, UniProtKB/Swiss-Prot Q6FCS7 (PURA_ACIAD)

Last modified February 9, 2010. Version 48. 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: ACIAD1258
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
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. 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: 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 – 439439Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000224247

Regions

Nucleotide binding13 – 197GTP Potential

Sites

Active site1411 By similarity
Active site1481 By similarity
Metal binding141Magnesium By similarity
Metal binding411Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FCS7-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 6390A56B8EF9918A

FASTA43947,238
        10         20         30         40         50         60 
MGKNVVVLGT QWGDEGKGKI VDLLTDQAAA VVRYQGGHNA GHTLVVGGKK TVLHLIPSGI 

        70         80         90        100        110        120 
LRENVLCLIG NGVVLSPAAL IKEMGILEEE GVPVKERLRI SPNCPLILPN HIALDQAREK 

       130        140        150        160        170        180 
KRGNAKIGTT GRGIGPAYED KVARRAVRVA DLVRGGAALE EKLQEMLELH NFQLTQFYGV 

       190        200        210        220        230        240 
EAVKFEDVLA LCNEWREVLA PLVIDVTKVL HDYRKEGKAI MFEGAQGSLL DIDHGTYPYV 

       250        260        270        280        290        300 
TSSNTTAGGV SSGSGMGPLH LDYVLGITKA YTTRVGAGPF PTELHYDAAT DTGDAIGRHL 

       310        320        330        340        350        360 
GTVGHEFGAS TGRQRRCGWF DAEILRRSVE VNSLSGICLT KLDVLDGLDE IKICVGYEDV 

       370        380        390        400        410        420 
DSGCAGSSDA VSFESLKPIY ETMPGWSEST VGLTSIDQLP ANALAYVKRI EQLIECPIDI 

       430 
ISTGPDRAET MILRHPFSA 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG68132.1.
RefSeqYP_045954.1.

3D structure databases

SMRQ6FCS7. Positions 2-439.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FCS7.

Genome annotation databases

GeneID2879345.
GenomeReviewsGene locus ACIAD1258 in contig CR543861_GR.
KEGGaci:ACIAD1258.
NMPDRfig|62977.3.peg.327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBQ6FCS7.

Enzyme and pathway databases

BioCycASP62977:ACIAD1258-MONOMER.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
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_ACIAD
AccessionPrimary (citable) accession number: Q6FCS7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 48 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