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Protein

Adenylosuccinate synthetase

Gene

purA

Organism
Yersinia pestis
Status
Reviewed-Annotation score: Annotation score: 4 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+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

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), Adenylosuccinate synthetase (purA)
  2. Adenylosuccinate lyase (purB), Adenylosuccinate lyase (purB), 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 acceptorUniRule annotation1
Metal bindingi14MagnesiumUniRule annotation1
Metal bindingi41Magnesium; via carbonyl oxygenUniRule annotation1
Active sitei42Proton donorUniRule annotation1
Binding sitei130IMPUniRule annotation1
Binding sitei144IMP; shared with dimeric partnerUniRule annotation1
Binding sitei225IMPUniRule annotation1
Binding sitei240IMPUniRule annotation1
Binding sitei304IMPUniRule annotation1
Binding sitei306GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 19GTPUniRule annotation7
Nucleotide bindingi41 – 43GTPUniRule annotation3
Nucleotide bindingi332 – 334GTPUniRule annotation3
Nucleotide bindingi415 – 417GTPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

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

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
Ordered Locus Names:YPO0378, y0635, YP_0534
OrganismiYersinia pestis
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000000815 Componenti: Chromosome
  • UP000001019 Componenti: Chromosome
  • UP000002490 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000952631 – 432Adenylosuccinate synthetaseAdd BLAST432

Proteomic databases

PRIDEiQ8ZIV7.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ8ZIV7. 1 interactor.
STRINGi187410.y0635.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Helixi17 – 25Combined sources9
Beta strandi29 – 33Combined sources5
Beta strandi42 – 46Combined sources5
Beta strandi49 – 56Combined sources8
Turni58 – 61Combined sources4
Beta strandi66 – 69Combined sources4
Helixi77 – 89Combined sources13
Helixi94 – 97Combined sources4
Beta strandi98 – 100Combined sources3
Helixi109 – 120Combined sources12
Helixi134 – 142Combined sources9
Helixi149 – 153Combined sources5
Helixi155 – 175Combined sources21
Helixi184 – 199Combined sources16
Helixi205 – 214Combined sources10
Beta strandi219 – 222Combined sources4
Helixi227 – 229Combined sources3
Turni231 – 233Combined sources3
Helixi246 – 248Combined sources3
Helixi249 – 253Combined sources5
Helixi257 – 259Combined sources3
Beta strandi262 – 273Combined sources12
Beta strandi275 – 277Combined sources3
Helixi286 – 294Combined sources9
Beta strandi307 – 312Combined sources6
Helixi313 – 323Combined sources11
Beta strandi327 – 331Combined sources5
Helixi333 – 336Combined sources4
Beta strandi340 – 349Combined sources10
Beta strandi355 – 358Combined sources4
Turni362 – 364Combined sources3
Beta strandi370 – 377Combined sources8
Helixi389 – 391Combined sources3
Helixi394 – 407Combined sources14
Beta strandi411 – 415Combined sources5
Beta strandi417 – 419Combined sources3
Beta strandi422 – 427Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HIDX-ray1.60A1-432[»]
ProteinModelPortaliQ8ZIV7.
SMRiQ8ZIV7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZIV7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 17IMP bindingUniRule annotation4
Regioni39 – 42IMP bindingUniRule annotation4
Regioni300 – 306Substrate bindingUniRule annotation7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

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

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.

Q8ZIV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKNVVVLGT QWGDEGKGKV VDLLTERAKY VVRYQGGHNA GHTLVINGEK
60 70 80 90 100
TVLHLIPSGI LRENVISIIG NGVVLAPDAL MKEMTELEAR GVPVRERLLL
110 120 130 140 150
SEACPLILPY HVALDNAREK ARGAKAIGTT GRGIGPAYED KVARRGLRVS
160 170 180 190 200
DLFNKETFAI KLKEIVEYHN FQLVHYYKEA AVDYQKVLDD VLAIADILTA
210 220 230 240 250
MVVDVSELLD NARKQGELIM FEGAQGTLLD IDHGTYPYVT SSNTTAGGVA
260 270 280 290 300
TGSGLGPRYV DYVLGIVKAY STRVGAGPFP TELNDETGEF LRKQGNEYGA
310 320 330 340 350
TTGRSRRTGW LDIVAVRRAV QINSLSGFCM TKLDVLDGLK EVKLCVGYRM
360 370 380 390 400
PDGREVDTTP LAAEGWEGIE PIYETMPGWS ETTFGVKEHS KLPQAALNYI
410 420 430
QRVEELTGVP IDIISTGPDR DETMILRDPF DA
Length:432
Mass (Da):47,278
Last modified:March 1, 2002 - v1
Checksum:i6A0C351ADC66BF4B
GO

Sequence cautioni

The sequence AAM84223 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAS60804 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL19060.1.
AE009952 Genomic DNA. Translation: AAM84223.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS60804.1. Different initiation.
PIRiAB0047.
RefSeqiWP_002209157.1. NZ_LQBA01000080.1.
YP_002345456.1. NC_003143.1.

Genome annotation databases

EnsemblBacteriaiAAM84223; AAM84223; y0635.
AAS60804; AAS60804; YP_0534.
GeneIDi1173224.
KEGGiype:YPO0378.
ypk:y0635.
ypm:YP_0534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL19060.1.
AE009952 Genomic DNA. Translation: AAM84223.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS60804.1. Different initiation.
PIRiAB0047.
RefSeqiWP_002209157.1. NZ_LQBA01000080.1.
YP_002345456.1. NC_003143.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HIDX-ray1.60A1-432[»]
ProteinModelPortaliQ8ZIV7.
SMRiQ8ZIV7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8ZIV7. 1 interactor.
STRINGi187410.y0635.

Proteomic databases

PRIDEiQ8ZIV7.

Protocols and materials databases

DNASUi1145582.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM84223; AAM84223; y0635.
AAS60804; AAS60804; YP_0534.
GeneIDi1173224.
KEGGiype:YPO0378.
ypk:y0635.
ypm:YP_0534.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.

Miscellaneous databases

EvolutionaryTraceiQ8ZIV7.

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_YERPE
AccessioniPrimary (citable) accession number: Q8ZIV7
Secondary accession number(s): Q0WJT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.