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P0A7D4

- PURA_ECOLI

UniProt

P0A7D4 - PURA_ECOLI

Protein

Adenylosuccinate synthetase

Gene

purA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.UniRule annotation

    Cofactori

    Binds 1 magnesium ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei14 – 141Proton acceptor
    Metal bindingi14 – 141Magnesium3 PublicationsUniRule annotation
    Metal bindingi41 – 411Magnesium; via carbonyl oxygen3 PublicationsUniRule annotation
    Active sitei42 – 421Proton donor
    Binding sitei130 – 1301IMP2 PublicationsUniRule annotation
    Binding sitei144 – 1441IMP; shared with dimeric partner2 PublicationsUniRule annotation
    Binding sitei225 – 2251IMP2 PublicationsUniRule annotation
    Binding sitei240 – 2401IMP2 PublicationsUniRule annotation
    Binding sitei304 – 3041IMP2 PublicationsUniRule annotation
    Binding sitei306 – 3061GTP1 PublicationUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 197GTP1 PublicationUniRule annotation
    Nucleotide bindingi41 – 433GTP1 PublicationUniRule annotation
    Nucleotide bindingi332 – 3343GTP1 PublicationUniRule annotation
    Nucleotide bindingi415 – 4173GTP1 PublicationUniRule annotation

    GO - Molecular functioni

    1. adenylosuccinate synthase activity Source: EcoCyc
    2. GTP binding Source: UniProtKB-HAMAP
    3. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
    2. adenosine biosynthetic process Source: EcoliWiki
    3. cellular response to DNA damage stimulus Source: EcoliWiki
    4. nucleobase-containing small molecule interconversion Source: EcoliWiki
    5. purine nucleotide biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ADENYLOSUCCINATE-SYN-MONOMER.
    ECOL316407:JW4135-MONOMER.
    MetaCyc:ADENYLOSUCCINATE-SYN-MONOMER.
    SABIO-RKP0A7D4.
    UniPathwayiUPA00075; UER00335.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate synthetaseUniRule annotation (EC:6.3.4.4UniRule annotation)
    Short name:
    AMPSaseUniRule annotation
    Short name:
    AdSSUniRule annotation
    Alternative name(s):
    IMP--aspartate ligaseUniRule annotation
    Gene namesi
    Name:purAUniRule annotation
    Synonyms:adeK
    Ordered Locus Names:b4177, JW4135
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10790. purA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131G → V: Significant reduction in activity. 1 Publication
    Mutagenesisi16 – 161G → V: Significant reduction in activity. 1 Publication
    Mutagenesisi17 – 171K → Q: Reduces catalytic efficiency by 50%. 1 Publication
    Mutagenesisi18 – 181G → V: Significant reduction in activity. 1 Publication
    Mutagenesisi19 – 191K → R: Significant reduction in activity. 1 Publication
    Mutagenesisi20 – 201I → T: Significant reduction in activity. 1 Publication
    Mutagenesisi141 – 1411K → I: Total loss of activity. 1 Publication
    Mutagenesisi144 – 1441R → L: Does not reduce catalytic efficiency. 1 Publication
    Mutagenesisi148 – 1481R → L: Reduced activity. 2 Publications
    Mutagenesisi304 – 3041R → L: Reduces catalytic efficiency by 87%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 432431Adenylosuccinate synthetasePRO_0000095174Add
    BLAST

    Proteomic databases

    PaxDbiP0A7D4.
    PRIDEiP0A7D4.

    2D gel databases

    SWISS-2DPAGEP0A7D4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7D4.

    Interactioni

    Subunit structurei

    Homodimer.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi852987. 1 interaction.
    DIPiDIP-36219N.
    IntActiP0A7D4. 2 interactions.
    MINTiMINT-1286548.
    STRINGi511145.b4177.

    Structurei

    Secondary structure

    1
    432
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1310
    Helixi17 – 248
    Turni25 – 273
    Beta strandi29 – 335
    Beta strandi42 – 465
    Beta strandi49 – 568
    Helixi58 – 614
    Beta strandi62 – 643
    Beta strandi66 – 694
    Helixi77 – 8913
    Helixi94 – 974
    Beta strandi98 – 1003
    Beta strandi104 – 1063
    Helixi109 – 12012
    Helixi123 – 1253
    Beta strandi126 – 1283
    Beta strandi131 – 1333
    Helixi134 – 1429
    Helixi149 – 1535
    Helixi155 – 17521
    Helixi184 – 19916
    Helixi205 – 21511
    Beta strandi219 – 2224
    Helixi227 – 2293
    Turni231 – 2333
    Beta strandi234 – 2385
    Helixi246 – 2483
    Helixi249 – 2535
    Helixi257 – 2593
    Beta strandi262 – 27312
    Beta strandi275 – 2773
    Helixi286 – 29510
    Turni300 – 3023
    Beta strandi307 – 3093
    Helixi313 – 32311
    Beta strandi327 – 3315
    Helixi333 – 3364
    Beta strandi340 – 34910
    Beta strandi355 – 3584
    Helixi363 – 3653
    Helixi366 – 3683
    Beta strandi370 – 3778
    Helixi389 – 3913
    Helixi394 – 40714
    Beta strandi411 – 4155
    Beta strandi417 – 4193
    Beta strandi422 – 4276
    Turni429 – 4313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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/B2-432[»]
    1HOOX-ray2.30A/B2-432[»]
    1HOPX-ray2.30A/B2-432[»]
    1JUYX-ray2.50A2-432[»]
    1KJXX-ray2.60A1-432[»]
    1KKBX-ray2.60A1-432[»]
    1KKFX-ray2.60A1-432[»]
    1KSZX-ray2.80A2-432[»]
    1NHTX-ray2.50A2-432[»]
    1QF4X-ray2.20A2-432[»]
    1QF5X-ray2.00A2-432[»]
    1SONX-ray2.55A2-432[»]
    1SOOX-ray2.60A2-432[»]
    2GCQX-ray2.00A2-432[»]
    ProteinModelPortaliP0A7D4.
    SMRiP0A7D4. Positions 2-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7D4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 174IMP binding
    Regioni39 – 424IMP binding
    Regioni300 – 3067Substrate binding

    Sequence similaritiesi

    Belongs to the adenylosuccinate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0104.
    HOGENOMiHOG000260959.
    KOiK01939.
    OMAiMKRAVQI.
    OrthoDBiEOG68Q0QG.
    PhylomeDBiP0A7D4.

    Family and domain databases

    HAMAPiMF_00011. Adenylosucc_synth.
    InterProiIPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11846. PTHR11846. 1 hit.
    PfamiPF00709. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SMARTiSM00788. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00184. purA. 1 hit.
    PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A7D4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK    50
    TVLHLIPSGI LRENVTSIIG NGVVLSPAAL MKEMKELEDR GIPVRERLLL 100
    SEACPLILDY HVALDNAREK ARGAKAIGTT GRGIGPAYED KVARRGLRVG 150
    DLFDKETFAE KLKEVMEYHN FQLVNYYKAE AVDYQKVLDD TMAVADILTS 200
    MVVDVSDLLD QARQRGDFVM FEGAQGTLLD IDHGTYPYVT SSNTTAGGVA 250
    TGSGLGPRYV DYVLGILKAY STRVGAGPFP TELFDETGEF LCKQGNEFGA 300
    TTGRRRRTGW LDTVAVRRAV QLNSLSGFCL TKLDVLDGLK EVKLCVAYRM 350
    PDGREVTTTP LAADDWKGVE PIYETMPGWS ESTFGVKDRS GLPQAALNYI 400
    KRIEELTGVP IDIISTGPDR TETMILRDPF DA 432
    Length:432
    Mass (Da):47,345
    Last modified:January 23, 2007 - v2
    Checksum:iAAA862CA0F80DA70
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti417 – 4171G → D in AAA24446. (PubMed:3058695)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04199 Genomic DNA. Translation: AAA24446.1.
    U14003 Genomic DNA. Translation: AAA97073.1.
    U00096 Genomic DNA. Translation: AAC77134.1.
    AP009048 Genomic DNA. Translation: BAE78178.1.
    PIRiS56402. AJECDS.
    RefSeqiNP_418598.1. NC_000913.3.
    YP_492319.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77134; AAC77134; b4177.
    BAE78178; BAE78178; BAE78178.
    GeneIDi12933702.
    948695.
    KEGGiecj:Y75_p4063.
    eco:b4177.
    PATRICi32123927. VBIEscCol129921_4308.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04199 Genomic DNA. Translation: AAA24446.1 .
    U14003 Genomic DNA. Translation: AAA97073.1 .
    U00096 Genomic DNA. Translation: AAC77134.1 .
    AP009048 Genomic DNA. Translation: BAE78178.1 .
    PIRi S56402. AJECDS.
    RefSeqi NP_418598.1. NC_000913.3.
    YP_492319.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ADE X-ray 2.00 A/B 2-432 [» ]
    1ADI X-ray 2.50 A/B 2-432 [» ]
    1CG0 X-ray 2.50 A 2-432 [» ]
    1CG1 X-ray 2.50 A 2-432 [» ]
    1CG3 X-ray 2.50 A 2-432 [» ]
    1CG4 X-ray 2.50 A 2-432 [» ]
    1CH8 X-ray 2.50 A 2-432 [» ]
    1CIB X-ray 2.30 A 2-432 [» ]
    1GIM X-ray 2.50 A 2-432 [» ]
    1GIN X-ray 2.80 A 2-432 [» ]
    1HON X-ray 2.30 A/B 2-432 [» ]
    1HOO X-ray 2.30 A/B 2-432 [» ]
    1HOP X-ray 2.30 A/B 2-432 [» ]
    1JUY X-ray 2.50 A 2-432 [» ]
    1KJX X-ray 2.60 A 1-432 [» ]
    1KKB X-ray 2.60 A 1-432 [» ]
    1KKF X-ray 2.60 A 1-432 [» ]
    1KSZ X-ray 2.80 A 2-432 [» ]
    1NHT X-ray 2.50 A 2-432 [» ]
    1QF4 X-ray 2.20 A 2-432 [» ]
    1QF5 X-ray 2.00 A 2-432 [» ]
    1SON X-ray 2.55 A 2-432 [» ]
    1SOO X-ray 2.60 A 2-432 [» ]
    2GCQ X-ray 2.00 A 2-432 [» ]
    ProteinModelPortali P0A7D4.
    SMRi P0A7D4. Positions 2-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852987. 1 interaction.
    DIPi DIP-36219N.
    IntActi P0A7D4. 2 interactions.
    MINTi MINT-1286548.
    STRINGi 511145.b4177.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    2D gel databases

    SWISS-2DPAGE P0A7D4.

    Proteomic databases

    PaxDbi P0A7D4.
    PRIDEi P0A7D4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77134 ; AAC77134 ; b4177 .
    BAE78178 ; BAE78178 ; BAE78178 .
    GeneIDi 12933702.
    948695.
    KEGGi ecj:Y75_p4063.
    eco:b4177.
    PATRICi 32123927. VBIEscCol129921_4308.

    Organism-specific databases

    EchoBASEi EB0783.
    EcoGenei EG10790. purA.

    Phylogenomic databases

    eggNOGi COG0104.
    HOGENOMi HOG000260959.
    KOi K01939.
    OMAi MKRAVQI.
    OrthoDBi EOG68Q0QG.
    PhylomeDBi P0A7D4.

    Enzyme and pathway databases

    UniPathwayi UPA00075 ; UER00335 .
    BioCyci EcoCyc:ADENYLOSUCCINATE-SYN-MONOMER.
    ECOL316407:JW4135-MONOMER.
    MetaCyc:ADENYLOSUCCINATE-SYN-MONOMER.
    SABIO-RK P0A7D4.

    Miscellaneous databases

    EvolutionaryTracei P0A7D4.
    PROi P0A7D4.

    Gene expression databases

    Genevestigatori P0A7D4.

    Family and domain databases

    HAMAPi MF_00011. Adenylosucc_synth.
    InterProi IPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR11846. PTHR11846. 1 hit.
    Pfami PF00709. Adenylsucc_synt. 1 hit.
    [Graphical view ]
    SMARTi SM00788. Adenylsucc_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00184. purA. 1 hit.
    PROSITEi PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiPURA_ECOLI
    AccessioniPrimary (citable) accession number: P0A7D4
    Secondary accession number(s): P12283, Q2M6C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3