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Protein

Adenylosuccinate synthetase

Gene

purA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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 + N6-(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-KW
  • metal ion binding Source: UniProtKB-KW

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

Keywordsi

Molecular functionLigase
Biological processPurine biosynthesis
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ADENYLOSUCCINATE-SYN-MONOMER
MetaCyc:ADENYLOSUCCINATE-SYN-MONOMER
BRENDAi6.3.4.4 2026
SABIO-RKiP0A7D4
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: EcoCyc
  • membrane Source: UniProtKB

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

Chemistry databases

DrugBankiDB02666 (C8-R)-Hydantocidin 5'-Phosphate
DB04460 (C8-S)-Hydantocidin 5'-Phosphate
DB02954 (Carboxyhydroxyamino)Ethanoic Acid
DB02682 2-Deamino-6-Deoxy-6thiophosphite-5'-Phosphate Guanosine
DB03146 2-Deazo-6-Thiophosphate Guanosine-5'-Monophosphate
DB02836 Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate
DB04315 Guanosine-5'-Diphosphate
DB02109 Hadacidin
DB02493 Hydantocidin-5'-Phosphate
DB04566 Inosinic Acid

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-2DPAGEiP0A7D4

PTM databases

CarbonylDBiP0A7D4

Interactioni

Subunit structurei

Homodimer.UniRule annotation3 Publications

Protein-protein interaction databases

BioGridi4262696, 52 interactors
852987, 1 interactor
DIPiDIP-36219N
IntActiP0A7D4, 3 interactors
STRINGi316385.ECDH10B_4372

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

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
OMAiSNAGHTV
PhylomeDBiP0A7D4

Family and domain databases

CDDicd03108 AdSS, 1 hit
HAMAPiMF_00011 Adenylosucc_synth, 1 hit
InterProiView protein in InterPro
IPR018220 Adenylosuccin_syn_GTP-bd
IPR033128 Adenylosuccin_syn_Lys_AS
IPR001114 Adenylosuccinate_synthetase
IPR027417 P-loop_NTPase
PANTHERiPTHR11846 PTHR11846, 1 hit
PfamiView protein in Pfam
PF00709 Adenylsucc_synt, 1 hit
SMARTiView protein in SMART
SM00788 Adenylsucc_synt, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00184 purA, 1 hit
PROSITEiView protein in PROSITE
PS01266 ADENYLOSUCCIN_SYN_1, 1 hit
PS00513 ADENYLOSUCCIN_SYN_2, 1 hit

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
PATRICifig|1411691.4.peg.2524

Similar proteinsi

Entry informationi

Entry nameiPURA_ECOLI
AccessioniPrimary (citable) accession number: P0A7D4
Secondary accession number(s): P12283, Q2M6C8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 126 of the entry and version 2 of the sequence. See 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

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