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B3H1V8 (PURA_ACTP7) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. 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:APP7_1133
OrganismActinobacillus pleuropneumoniae serotype 7 (strain AP76) [Complete proteome] [HAMAP]
Taxonomic identifier537457 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length432 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 – 432432Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000089264

Regions

Nucleotide binding13 – 197GTP By similarity
Nucleotide binding41 – 433GTP By similarity
Nucleotide binding332 – 3343GTP By similarity
Nucleotide binding415 – 4173GTP By similarity
Region14 – 174IMP binding By similarity
Region39 – 424IMP binding By similarity
Region300 – 3067Substrate binding By similarity

Sites

Active site141Proton acceptor By similarity
Active site421Proton donor By similarity
Metal binding141Magnesium By similarity
Metal binding411Magnesium; via carbonyl oxygen By similarity
Binding site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2251IMP By similarity
Binding site2401IMP By similarity
Binding site3041IMP By similarity
Binding site3061GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3H1V8 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 79B71EA169C15B0D

FASTA43247,443
        10         20         30         40         50         60 
MGKSVAILGA QWGDEGKGKI VDLLTDRVKY VVRYQGGHNA GHTLIINGEK TVLRLIPSGI 

        70         80         90        100        110        120 
LRDNVTCLIG NGVVLSPEAL MKEMGELEAR GINVRDRLKI SEACPLILPY HVAMDHAREA 

       130        140        150        160        170        180 
ALGKNKIGTT GRGIGPAYED KVARRGLRVS DLFDKEAFAE KLKDILDYYN FQLVHYYKVE 

       190        200        210        220        230        240 
PVDFQKTLDD VFAIADVIKG MVADVTTLLH QARKDGVNIL FEGAQGTMLD IDHGTYPFVT 

       250        260        270        280        290        300 
SSNTTAGGVA TGSGFGPRNL DYVLGIIKAY CTRVGSGPFT TELFDEVGAE IARKGNEFGA 

       310        320        330        340        350        360 
VTGRPRRCGW FDAVAVRRAV QINSISGFCM TKLDVLDGFE ELKICTAYKM PNGEIVEYAP 

       370        380        390        400        410        420 
MAAKDWKGVE PIYETMPGWS ENTFRVTKRE ELPQAALDYI KRIEELVGVP VDILSTGPDR 

       430 
VETMILRDPF AA

« Hide

References

[1]"Genome and proteome analysis of A. pleuropneumoniae serotype 7."
Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N., Tegetmeyer H., Singh M., Gerlach G.F.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AP76.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001091 Genomic DNA. Translation: ACE61785.1.
RefSeqYP_001968927.1. NC_010939.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3H1V8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6396171.
GenomeReviewsGene locus APP7_1133 in contig CP001091_GR.
KEGGapa:APP7_1133.
PATRIC20755911. VBIActPle116979_1157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
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_ACTP7
AccessionPrimary (citable) accession number: B3H1V8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 23 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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