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Reviewed, UniProtKB/Swiss-Prot Q7MAX9 (PURA2_PHOLL)

Last modified November 3, 2009. Version 45. 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 2
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase 2
    AdSS 2
    AMPSase 2
Gene names
Name: purA2
Ordered Locus Names: plu4577
OrganismPhotorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]
Taxonomic identifier141679 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length432 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 – 432432Adenylosuccinate synthetase 2 HAMAP MF_00011
PRO_0000095208

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
Q7MAX9-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: B798323C9425F2CA

FASTA43247,240
        10         20         30         40         50         60 
MGKNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI 

        70         80         90        100        110        120 
LRENVISIIA NGVVLAPDAL MKEMNALESR GIPVRERLLI SEACPLILPY HVALDNAREK 

       130        140        150        160        170        180 
ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFDKEAFAV KLKEIIEYHN FQLVNYYKEP 

       190        200        210        220        230        240 
AVDYQKTLDE IMAVADILTD MVVDVSDLLY KATQKGELVM FEGAQGTLLD IDHGTYPYVT 

       250        260        270        280        290        300 
SSNTTAGGVA TGSGLGPCYV DYVLGIIKAY STRVGAGPFP TELFDETGGY LREKGQEFGA 

       310        320        330        340        350        360 
TTGRSRRTGW LDIIAIRRAV QINSLSGFCM TKLDVLDGLK EVKICTGYRM PDGSVIETTP 

       370        380        390        400        410        420 
LAADDWEGIE PVYETMPGWN ESTFGVKEHR KLPQAALNYI KRVEELTGVP VDIISTGPDR 

       430 
SETIILRDPF DA 

« Hide

Cross-references

Sequence databases

BX571874 Genomic DNA. Translation: CAE16949.1.
RefSeqNP_931741.1.

3D structure databases

SMRQ7MAX9. Positions 2-432.
ModBaseSearch...

Genome annotation databases

GeneID2804601.
GenomeReviewsGene locus plu4577 in contig BX470251_GR.
KEGGplu:plu4577.
NMPDRfig|243265.1.peg.4364.

Organism-specific databases

PhotoListplu4577.
CMRSearch...

Phylogenomic databases

HOGENOMQ7MAX9.
OMAYVLGIIK.

Enzyme and pathway databases

BioCycPLUM243265:PLU4577-MON.
BRENDA6.3.4.4. 308689.

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 namePURA2_PHOLL
AccessionPrimary (citable) accession number: Q7MAX9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: December 15, 2003
Last modified: November 3, 2009
This is version 45 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