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P0A7D4

- PURA_ECOLI

UniProt

P0A7D4 - PURA_ECOLI

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Protein

Adenylosuccinate synthetase

Gene

purA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Mg2+Note: Binds 1 Mg(2+) 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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0A7D4.
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

        10         20         30         40         50
MGNNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK
60 70 80 90 100
TVLHLIPSGI LRENVTSIIG NGVVLSPAAL MKEMKELEDR GIPVRERLLL
110 120 130 140 150
SEACPLILDY HVALDNAREK ARGAKAIGTT GRGIGPAYED KVARRGLRVG
160 170 180 190 200
DLFDKETFAE KLKEVMEYHN FQLVNYYKAE AVDYQKVLDD TMAVADILTS
210 220 230 240 250
MVVDVSDLLD QARQRGDFVM FEGAQGTLLD IDHGTYPYVT SSNTTAGGVA
260 270 280 290 300
TGSGLGPRYV DYVLGILKAY STRVGAGPFP TELFDETGEF LCKQGNEFGA
310 320 330 340 350
TTGRRRRTGW LDTVAVRRAV QLNSLSGFCL TKLDVLDGLK EVKLCVAYRM
360 370 380 390 400
PDGREVTTTP LAADDWKGVE PIYETMPGWS ESTFGVKDRS GLPQAALNYI
410 420 430
KRIEELTGVP IDIISTGPDR TETMILRDPF DA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.

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.
InParanoidi P0A7D4.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 102 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