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B1XIL5 (PURA_SYNP2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:SYNPCC7002_A0882
OrganismSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]
Taxonomic identifier32049 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechococcus

Protein attributes

Sequence length443 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 commited step in the biosynthesis of AMP from IMP By similarity. 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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000089345

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding330 – 3323GTP By similarity
Nucleotide binding412 – 4143GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region298 – 3047Substrate 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 site1281IMP By similarity
Binding site1421IMP; shared with dimeric partner By similarity
Binding site2231IMP By similarity
Binding site2381IMP By similarity
Binding site3021IMP By similarity
Binding site3041GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1XIL5 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 560618524B7C6600

FASTA44348,224
        10         20         30         40         50         60 
MANVVVIGAQ WGDEGKGKIT DLLSKSADVV VRSQGGVNAG HTVVVQGQTF KLHLIPSGIL 

        70         80         90        100        110        120 
YPDTECIIGS GTVIDPKVLL EEIDQLHRLN VSTENLFISQ TAHVTMPYHR LIDGASEEMR 

       130        140        150        160        170        180 
GDRKIGTTGR GIGPTYADKS ERTGVRVLDL MDLDNSQDKF VWAIKYKNVI LEKLYDLPPL 

       190        200        210        220        230        240 
DPQEVIEEYR AYADALRPHV VDSSLKVFEG VNAKKNILFE GAQGTLLDID HGTYPYVTSS 

       250        260        270        280        290        300 
NPIAGGACVG AGIGPTIIDR VIGVAKAYTT RVGEGPFPTE LDDEIGELLG HVGAEFGTTT 

       310        320        330        340        350        360 
GRRRRCGWFD AVIGRYAARI NGLDCLAITK LDVLDSLDEI KVCVAYEIDG EACEHFPSNA 

       370        380        390        400        410        420 
NLFARCQPIY KTMPGWKQPT SDCRSLDELP KEALAYLKFL AELMDVPIAI VSLGAGREQT 

       430        440 
IIVEDPIHGP KRALLDRNGE PIG 

« Hide

References

[1]"Complete sequence of Synechococcus sp. PCC 7002."
Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27264 / PCC 7002 / PR-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000951 Genomic DNA. Translation: ACA98886.1.
RefSeqYP_001734142.1. NC_010475.1.

3D structure databases

ProteinModelPortalB1XIL5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1XIL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6056299.
GenomeReviewsGene locus SYNPCC7002_A0882 in contig CP000951_GR.
KEGGsyp:SYNPCC7002_A0882.
PATRIC23816278. VBISynSp37135_1096.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBB1XIL5.
ProtClustDBPRK01117.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
KOK01939.
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_SYNP2
AccessionPrimary (citable) accession number: B1XIL5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 28 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