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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei14 – 141Proton acceptorUniRule annotation
Metal bindingi14 – 141MagnesiumUniRule annotation
Metal bindingi41 – 411Magnesium; via carbonyl oxygenUniRule annotation
Active sitei42 – 421Proton donorUniRule annotation
Binding sitei130 – 1301IMPUniRule annotation
Binding sitei144 – 1441IMP; shared with dimeric partnerUniRule annotation
Binding sitei225 – 2251IMPUniRule annotation
Binding sitei240 – 2401IMPUniRule annotation
Binding sitei304 – 3041IMPUniRule annotation
Binding sitei306 – 3061GTPUniRule annotation

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

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

BioCyciYPES214092:GKDD-375-MONOMER.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Adenylosuccinate synthetasePRO_0000095263Add
BLAST

Proteomic databases

PRIDEiQ8ZIV7.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ8ZIV7. 1 interaction.
STRINGi187410.y0635.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Helixi17 – 259Combined sources
Beta strandi29 – 335Combined sources
Beta strandi42 – 465Combined sources
Beta strandi49 – 568Combined sources
Turni58 – 614Combined sources
Beta strandi66 – 694Combined sources
Helixi77 – 8913Combined sources
Helixi94 – 974Combined sources
Beta strandi98 – 1003Combined sources
Helixi109 – 12012Combined sources
Helixi134 – 1429Combined sources
Helixi149 – 1535Combined sources
Helixi155 – 17521Combined sources
Helixi184 – 19916Combined sources
Helixi205 – 21410Combined sources
Beta strandi219 – 2224Combined sources
Helixi227 – 2293Combined sources
Turni231 – 2333Combined sources
Helixi246 – 2483Combined sources
Helixi249 – 2535Combined sources
Helixi257 – 2593Combined sources
Beta strandi262 – 27312Combined sources
Beta strandi275 – 2773Combined sources
Helixi286 – 2949Combined sources
Beta strandi307 – 3126Combined sources
Helixi313 – 32311Combined sources
Beta strandi327 – 3315Combined sources
Helixi333 – 3364Combined sources
Beta strandi340 – 34910Combined sources
Beta strandi355 – 3584Combined sources
Turni362 – 3643Combined sources
Beta strandi370 – 3778Combined sources
Helixi389 – 3913Combined sources
Helixi394 – 40714Combined sources
Beta strandi411 – 4155Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi422 – 4276Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HIDX-ray1.60A1-432[»]
ProteinModelPortaliQ8ZIV7.
SMRiQ8ZIV7. Positions 2-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZIV7.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

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

Family and domain databases

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_LQAY01000087.1.
YP_002345456.1. NC_003143.1.

Genome annotation databases

EnsemblBacteriaiAAM84223; AAM84223; y0635.
AAS60804; AAS60804; YP_0534.
GeneIDi1173224.
KEGGiype:YPO0378.
ypj:CH55_3385.
ypk:y0635.
ypl:CH46_536.
ypm:YP_0534.
ypv:BZ15_3193.
ypw:CH59_1483.

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_LQAY01000087.1.
YP_002345456.1. NC_003143.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HIDX-ray1.60A1-432[»]
ProteinModelPortaliQ8ZIV7.
SMRiQ8ZIV7. Positions 2-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8ZIV7. 1 interaction.
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.
ypj:CH55_3385.
ypk:y0635.
ypl:CH46_536.
ypm:YP_0534.
ypv:BZ15_3193.
ypw:CH59_1483.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.
BioCyciYPES214092:GKDD-375-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8ZIV7.

Family and domain databases

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: September 7, 2016
This is version 113 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.