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Protein

Adenylosuccinate synthetase

Gene

purA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from IMP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase (purA)
  2. Adenylosuccinate lyase (purB)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei14Proton acceptor1
Metal bindingi14MagnesiumUniRule annotation3 Publications1
Metal bindingi41Magnesium; via carbonyl oxygenUniRule annotation3 Publications1
Active sitei42Proton donor1
Binding sitei130IMPUniRule annotation2 Publications1
Binding sitei144IMP; shared with dimeric partnerUniRule annotation2 Publications1
Binding sitei225IMPUniRule annotation2 Publications1
Binding sitei240IMPUniRule annotation2 Publications1
Binding sitei304IMPUniRule annotation2 Publications1
Binding sitei306GTPUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 19GTPUniRule annotation1 Publication7
Nucleotide bindingi41 – 43GTPUniRule annotation1 Publication3
Nucleotide bindingi332 – 334GTPUniRule annotation1 Publication3
Nucleotide bindingi415 – 417GTPUniRule annotation1 Publication3

GO - Molecular functioni

  • adenylosuccinate synthase activity Source: EcoCyc
  • GTP binding Source: UniProtKB-HAMAP
  • magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • 'de novo' AMP biosynthetic process Source: GO_Central
  • adenosine biosynthetic process Source: EcoliWiki
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • IMP metabolic process Source: GO_Central
  • nucleobase-containing small molecule interconversion Source: EcoliWiki
  • 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.
BRENDAi6.3.4.4. 2026.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10790. purA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13G → V: Significant reduction in activity. 1 Publication1
Mutagenesisi16G → V: Significant reduction in activity. 1 Publication1
Mutagenesisi17K → Q: Reduces catalytic efficiency by 50%. 1 Publication1
Mutagenesisi18G → V: Significant reduction in activity. 1 Publication1
Mutagenesisi19K → R: Significant reduction in activity. 1 Publication1
Mutagenesisi20I → T: Significant reduction in activity. 1 Publication1
Mutagenesisi141K → I: Total loss of activity. 1 Publication1
Mutagenesisi144R → L: Does not reduce catalytic efficiency. 1 Publication1
Mutagenesisi148R → L: Reduced activity. 1 Publication1
Mutagenesisi304R → L: Reduces catalytic efficiency by 87%. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000951742 – 432Adenylosuccinate synthetaseAdd BLAST431

Proteomic databases

EPDiP0A7D4.
PaxDbiP0A7D4.
PRIDEiP0A7D4.

2D gel databases

SWISS-2DPAGEP0A7D4.

Interactioni

Subunit structurei

Homodimer.UniRule annotation3 Publications

Protein-protein interaction databases

BioGridi4262696. 26 interactors.
852987. 1 interactor.
DIPiDIP-36219N.
IntActiP0A7D4. 2 interactors.
MINTiMINT-1286548.
STRINGi511145.b4177.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 13Combined sources10
Helixi17 – 24Combined sources8
Turni25 – 27Combined sources3
Beta strandi29 – 33Combined sources5
Beta strandi42 – 46Combined sources5
Beta strandi49 – 56Combined sources8
Helixi58 – 61Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi66 – 69Combined sources4
Helixi77 – 89Combined sources13
Helixi94 – 97Combined sources4
Beta strandi98 – 100Combined sources3
Beta strandi104 – 106Combined sources3
Helixi109 – 120Combined sources12
Helixi123 – 125Combined sources3
Beta strandi126 – 128Combined sources3
Beta strandi131 – 133Combined sources3
Helixi134 – 142Combined sources9
Helixi149 – 153Combined sources5
Helixi155 – 175Combined sources21
Helixi184 – 199Combined sources16
Helixi205 – 215Combined sources11
Beta strandi219 – 222Combined sources4
Helixi227 – 229Combined sources3
Turni231 – 233Combined sources3
Beta strandi234 – 238Combined sources5
Helixi246 – 248Combined sources3
Helixi249 – 253Combined sources5
Helixi257 – 259Combined sources3
Beta strandi262 – 273Combined sources12
Beta strandi275 – 277Combined sources3
Helixi286 – 295Combined sources10
Turni300 – 302Combined sources3
Beta strandi307 – 309Combined sources3
Helixi313 – 323Combined sources11
Beta strandi327 – 331Combined sources5
Helixi333 – 336Combined sources4
Beta strandi340 – 349Combined sources10
Beta strandi355 – 358Combined sources4
Helixi363 – 365Combined sources3
Helixi366 – 368Combined sources3
Beta strandi370 – 377Combined sources8
Helixi389 – 391Combined sources3
Helixi394 – 407Combined sources14
Beta strandi411 – 415Combined sources5
Beta strandi417 – 419Combined sources3
Beta strandi422 – 427Combined sources6
Turni429 – 431Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7D4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 17IMP binding4
Regioni39 – 42IMP binding4
Regioni300 – 306Substrate binding7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C91. Bacteria.
COG0104. LUCA.
HOGENOMiHOG000260959.
InParanoidiP0A7D4.
KOiK01939.
OMAiFHHAKPI.
PhylomeDBiP0A7D4.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_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)DescriptionActionsGraphical viewLength
Sequence conflicti417G → D in AAA24446 (PubMed:3058695).Curated1

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.
WP_000527955.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77134; AAC77134; b4177.
BAE78178; BAE78178; BAE78178.
GeneIDi948695.
KEGGiecj:JW4135.
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.
PIRiS56402. AJECDS.
RefSeqiNP_418598.1. NC_000913.3.
WP_000527955.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262696. 26 interactors.
852987. 1 interactor.
DIPiDIP-36219N.
IntActiP0A7D4. 2 interactors.
MINTiMINT-1286548.
STRINGi511145.b4177.

2D gel databases

SWISS-2DPAGEP0A7D4.

Proteomic databases

EPDiP0A7D4.
PaxDbiP0A7D4.
PRIDEiP0A7D4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77134; AAC77134; b4177.
BAE78178; BAE78178; BAE78178.
GeneIDi948695.
KEGGiecj:JW4135.
eco:b4177.
PATRICi32123927. VBIEscCol129921_4308.

Organism-specific databases

EchoBASEiEB0783.
EcoGeneiEG10790. purA.

Phylogenomic databases

eggNOGiENOG4105C91. Bacteria.
COG0104. LUCA.
HOGENOMiHOG000260959.
InParanoidiP0A7D4.
KOiK01939.
OMAiFHHAKPI.
PhylomeDBiP0A7D4.

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.
BioCyciEcoCyc:ADENYLOSUCCINATE-SYN-MONOMER.
ECOL316407:JW4135-MONOMER.
MetaCyc:ADENYLOSUCCINATE-SYN-MONOMER.
BRENDAi6.3.4.4. 2026.
SABIO-RKP0A7D4.

Miscellaneous databases

EvolutionaryTraceiP0A7D4.
PROiP0A7D4.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_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]
ProtoNetiSearch...

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 2, 2016
This is version 117 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.