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P0A7D4

- PURA_ECOLI

UniProt

P0A7D4 - PURA_ECOLI

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Protein
Adenylosuccinate synthetase
Gene
purA, adeK, b4177, JW4135
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.UniRule annotation

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 – 141Magnesium
Metal bindingi41 – 411Magnesium; via carbonyl oxygen
Active sitei42 – 421Proton donor
Binding sitei130 – 1301IMP
Binding sitei144 – 1441IMP; shared with dimeric partner
Binding sitei225 – 2251IMP
Binding sitei240 – 2401IMP
Binding sitei304 – 3041IMP
Binding sitei306 – 3061GTP

Regions

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

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-HAMAP
  2. adenylosuccinate synthase activity Source: EcoCyc
  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 synthetase (EC:6.3.4.4)
Short name:
AMPSase
Short name:
AdSS
Alternative name(s):
IMP--aspartate ligase
Gene namesi
Name:purA
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

Cytoplasm UniRule annotation

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 432431Adenylosuccinate synthetaseUniRule annotation
PRO_0000095174Add
BLAST

Proteomic databases

PaxDbiP0A7D4.
PRIDEiP0A7D4.

2D gel databases

SWISS-2DPAGEP0A7D4.

Expressioni

Gene expression databases

GenevestigatoriP0A7D4.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP0A7D4.

Family & Domainsi

Region

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti417 – 4171G → D in AAA24446. 1 Publication

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

« 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: July 9, 2014
This is version 99 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

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