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Q03TS9 (PURA_LACBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:LVIS_0227
OrganismLactobacillus brevis (strain ATCC 367 / JCM 1170) [Complete proteome] [HAMAP]
Taxonomic identifier387344 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

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 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 – 428428Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000000841

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding329 – 3313GTP By similarity
Nucleotide binding411 – 4133GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region297 – 3037Substrate 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 site1271IMP By similarity
Binding site1411IMP; shared with dimeric partner By similarity
Binding site2221IMP By similarity
Binding site2371IMP By similarity
Binding site3011IMP By similarity
Binding site3031GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03TS9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 11CC669F31DF5E25

FASTA42846,870
        10         20         30         40         50         60 
MSSTVVVGSQ WGDEGKGKIT DFLSEKADVI ARYQGGDNAG HTIVFNGQTF KLRLIPSGIF 

        70         80         90        100        110        120 
YADKTSVIGN GVVLNPQSLI EELTYLHDNG VATDNLRISD RAHVILPYHI LLDQAQEKAK 

       130        140        150        160        170        180 
ASKIGTTNKG IGPAYMDKAE RIGIRVADLL DHDIFAEKLH QNLIEKNKVL TKLYDEEPLN 

       190        200        210        220        230        240 
YDDIFETYYA LGQQLKGYVT DTSVVINDAL DAGKNVLFEG AQGVMLDIDH GTYPFVTSSN 

       250        260        270        280        290        300 
PVAGGVTIGS GVGPTKIDHV VGVCKAYTSR VGDGPFPTEL FDEIGDTIRE TGHEYGTVTK 

       310        320        330        340        350        360 
RPRRIGWFDS VVLRHAKRVS GLTTLSLNCL DVLTGLKTVK ICKAYQLNGE TIYHYPASLV 

       370        380        390        400        410        420 
DLDACQPVYE ELPGWDEDIT HCRSVAELPA NAQTYVKRLA ELVGVEIATL SVGPDREQTN 


ILQDVWNA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000416 Genomic DNA. Translation: ABJ63393.1.
RefSeqYP_794424.1. NC_008497.1.

3D structure databases

ProteinModelPortalQ03TS9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ03TS9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4413049.
GenomeReviewsGene locus LVIS_0227 in contig CP000416_GR.
KEGGlbr:LVIS_0227.
NMPDRfig|387344.8.peg.219.
PATRIC22199422. VBILacBre134470_0223.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBQ03TS9.

Enzyme and pathway databases

BioCycLBRE387344:LVIS_0227-MONOMER.

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_LACBA
AccessionPrimary (citable) accession number: Q03TS9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: January 25, 2012
This is version 36 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