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P0A7D4 (PURA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:adeK
Ordered Locus Names:b4177, JW4135
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_00011

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_00011

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_00011

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.6
Chain2 – 432431Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_0000095174

Regions

Nucleotide binding13 – 197GTP HAMAP-Rule MF_00011
Nucleotide binding41 – 433GTP HAMAP-Rule MF_00011
Nucleotide binding332 – 3343GTP HAMAP-Rule MF_00011
Nucleotide binding415 – 4173GTP HAMAP-Rule MF_00011
Region14 – 174IMP binding HAMAP-Rule MF_00011
Region39 – 424IMP binding HAMAP-Rule MF_00011
Region300 – 3067Substrate binding HAMAP-Rule MF_00011

Sites

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

Experimental info

Mutagenesis131G → V: Significant reduction in activity.
Mutagenesis161G → V: Significant reduction in activity.
Mutagenesis171K → Q: Reduces catalytic efficiency by 50%.
Mutagenesis181G → V: Significant reduction in activity.
Mutagenesis191K → R: Significant reduction in activity.
Mutagenesis201I → T: Significant reduction in activity.
Mutagenesis1411K → I: Total loss of activity.
Mutagenesis1441R → L: Does not reduce catalytic efficiency.
Mutagenesis1481R → L: Reduced activity. Ref.5
Mutagenesis3041R → L: Reduces catalytic efficiency by 87%.
Sequence conflict4171G → D in AAA24446. Ref.1

Secondary structure

......................................................................................... 432
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7D4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AAA862CA0F80DA70

FASTA43247,345
        10         20         30         40         50         60 
MGNNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI 

        70         80         90        100        110        120 
LRENVTSIIG NGVVLSPAAL MKEMKELEDR GIPVRERLLL SEACPLILDY HVALDNAREK 

       130        140        150        160        170        180 
ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFDKETFAE KLKEVMEYHN FQLVNYYKAE 

       190        200        210        220        230        240 
AVDYQKVLDD TMAVADILTS MVVDVSDLLD QARQRGDFVM FEGAQGTLLD IDHGTYPYVT 

       250        260        270        280        290        300 
SSNTTAGGVA TGSGLGPRYV DYVLGILKAY STRVGAGPFP TELFDETGEF LCKQGNEFGA 

       310        320        330        340        350        360 
TTGRRRRTGW LDTVAVRRAV QLNSLSGFCL TKLDVLDGLK EVKLCVAYRM PDGREVTTTP 

       370        380        390        400        410        420 
LAADDWKGVE PIYETMPGWS ESTFGVKDRS GLPQAALNYI KRIEELTGVP IDIISTGPDR 

       430 
TETMILRDPF DA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12."
Wolfe S.A., Smith J.M.
J. Biol. Chem. 263:19147-19153(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
Strain: K12.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis."
Dong Q., Liu F., Myers A.M., Fromm H.J.
J. Biol. Chem. 266:12228-12233(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 146-148, MUTAGENESIS OF ARG-148.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10.
Strain: K12 / EMG2.
[7]"Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal 5'-phosphate. Identification of an active site lysyl residue."
Dong Q., Fromm H.J.
J. Biol. Chem. 265:6235-6240(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE LYS-141.
[8]"Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase."
Liu F., Dong Q., Fromm H.J.
J. Biol. Chem. 267:2388-2392(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[9]"Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli."
Silva M.M., Poland B.W., Hoffman C.R., Fromm H.J., Honzatko R.B.
J. Mol. Biol. 254:431-446(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 417.
[10]"Refined crystal structure of adenylosuccinate synthetase from Escherichia coli complexed with hydantocidin 5'-phosphate, GDP, HPO4(2-), Mg2+, and hadacidin."
Poland B.W., Lee S.F., Subramanian M.V., Siehl D.L., Anderson R.J., Fromm H.J., Honzatko R.B.
Biochemistry 35:15753-15759(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GDP; MAGNESIUM; SUBSTRATE ANALOG AND INHIBITOR.
[11]"Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli."
Poland B.W., Hou Z., Bruns C., Fromm H.J., Honzatko R.B.
J. Biol. Chem. 271:15407-15413(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-431.
[12]"Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+."
Poland B.W., Fromm H.J., Honzatko R.B.
J. Mol. Biol. 264:1013-1027(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP; IMP; MAGNESIUM AND SUBSTRATE ANALOG.
[13]"The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase."
Fonne-Pfister R., Chemla P., Ward E., Girardet M., Kreuz K.E., Honzatko R.B., Fromm H.J., Schaer H.-P., Gruetter M.G., Cowan-Jacob S.W.
Proc. Natl. Acad. Sci. U.S.A. 93:9431-9436(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-431.
[14]"Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli."
Poland B.W., Bruns C., Fromm H.J., Honzatko R.B.
J. Biol. Chem. 272:15200-15205(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-431.
[15]"An enzyme-bound bisubstrate hybrid inhibitor of adenylosuccinate synthetase."
Hanessian S., Lu P.P., Sanceau J.Y., Chemla P., Gohda K., Fonne-Pfister R., Prade L., Cowan-Jacob S.W.
Angew. Chem. Int. Ed. Engl. 38:3159-3162(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[16]"Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli."
Choe J.Y., Poland B.W., Fromm H.J., Honzatko R.B.
Biochemistry 38:6953-6961(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-17; LEU-144 AND LEU-304 IN COMPLEX WITH GTP; IMP; MAGNESIUM AND SUBSTRATE ANALOG.
[17]"Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase."
Hou Z., Cashel M., Fromm H.J., Honzatko R.B.
J. Biol. Chem. 274:17505-17510(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[18]"IMP alone organizes the active site of adenylosuccinate synthetase from Escherichia coli."
Hou Z., Wang W., Fromm H.J., Honzatko R.B.
J. Biol. Chem. 277:5970-5976(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-432.
[19]"Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases."
Iancu C.V., Zhou Y., Borza T., Fromm H.J., Honzatko R.B.
Biochemistry 45:11703-11711(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-431.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04199 Genomic DNA. Translation: AAA24446.1.
U14003 Genomic DNA. Translation: AAA97073.1.
U00096 Genomic DNA. Translation: AAC77134.1.
AP009048 Genomic DNA. Translation: BAE78178.1.
PIRAJECDS. S56402.
RefSeqNP_418598.1. NC_000913.3.
YP_492319.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ADEX-ray2.00A/B2-432[»]
1ADIX-ray2.50A/B2-432[»]
1CG0X-ray2.50A2-432[»]
1CG1X-ray2.50A2-432[»]
1CG3X-ray2.50A2-432[»]
1CG4X-ray2.50A2-432[»]
1CH8X-ray2.50A2-432[»]
1CIBX-ray2.30A2-432[»]
1GIMX-ray2.50A2-432[»]
1GINX-ray2.80A2-432[»]
1HONX-ray2.30A/B2-431[»]
1HOOX-ray2.30A/B2-431[»]
1HOPX-ray2.30A/B2-431[»]
1JUYX-ray2.50A2-432[»]
1KJXX-ray2.60A1-432[»]
1KKBX-ray2.60A1-432[»]
1KKFX-ray2.60A1-432[»]
1KSZX-ray2.80A2-431[»]
1NHTX-ray2.50A2-431[»]
1QF4X-ray2.20A2-432[»]
1QF5X-ray2.00A2-432[»]
1SONX-ray2.55A2-431[»]
1SOOX-ray2.60A2-431[»]
2GCQX-ray2.00A2-431[»]
ProteinModelPortalP0A7D4.
SMRP0A7D4. Positions 2-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852987. 1 interaction.
DIPDIP-36219N.
IntActP0A7D4. 2 interactions.
MINTMINT-1286548.
STRING511145.b4177.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

2D gel databases

SWISS-2DPAGEP0A7D4.

Proteomic databases

PaxDbP0A7D4.
PRIDEP0A7D4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77134; AAC77134; b4177.
BAE78178; BAE78178; BAE78178.
GeneID12933702.
948695.
KEGGecj:Y75_p4063.
eco:b4177.
PATRIC32123927. VBIEscCol129921_4308.

Organism-specific databases

EchoBASEEB0783.
EcoGeneEG10790. purA.

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMADYVVRYQ.
OrthoDBEOG68Q0QG.
PhylomeDBP0A7D4.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycEcoCyc:ADENYLOSUCCINATE-SYN-MONOMER.
ECOL316407:JW4135-MONOMER.
MetaCyc:ADENYLOSUCCINATE-SYN-MONOMER.
SABIO-RKP0A7D4.
UniPathwayUPA00075; UER00335.

Gene expression databases

GenevestigatorP0A7D4.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7D4.
PROP0A7D4.

Entry information

Entry namePURA_ECOLI
AccessionPrimary (citable) accession number: P0A7D4
Secondary accession number(s): P12283, Q2M6C8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene