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Protein

Adenylosuccinate synthetase, chloroplastic

Gene
N/A
Organism
Triticum aestivum (Wheat)
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 and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).By similarity

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, chloroplastic, Adenylosuccinate synthetase, chloroplastic (PURA), Adenylosuccinate synthetase, chloroplastic (PURA), Adenylosuccinate synthetase, chloroplastic (PURA)
  2. no protein annotated in this organism
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 sitei64Proton acceptorUniRule annotation1
Metal bindingi64MagnesiumUniRule annotation1
Metal bindingi91Magnesium; via carbonyl oxygenUniRule annotation1
Active sitei92Proton donorUniRule annotation1
Binding sitei181IMPUniRule annotation1
Binding sitei195IMP; shared with dimeric partnerUniRule annotation1
Binding sitei275IMPUniRule annotation1
Binding sitei290IMPUniRule annotation1
Binding sitei354IMPUniRule annotation1
Binding sitei356GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi63 – 69GTP7
Nucleotide bindingi91 – 93GTP3
Nucleotide bindingi382 – 384GTP3
Nucleotide bindingi465 – 467GTP3

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

BRENDAi6.3.4.4. 6500.
UniPathwayiUPA00075; UER00335.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetase, chloroplasticUniRule annotation (EC:6.3.4.4UniRule annotation)
Short name:
AMPSaseUniRule annotation
Short name:
AdSSUniRule annotation
Alternative name(s):
IMP--aspartate ligaseUniRule annotation
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum
Proteomesi
  • UP000019116 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000029872? – 476Adenylosuccinate synthetase, chloroplastic
Transit peptidei‹1 – ?Chloroplast

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi47 – 49Combined sources3
Beta strandi53 – 59Combined sources7
Beta strandi61 – 63Combined sources3
Helixi67 – 74Combined sources8
Helixi75 – 77Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi92 – 95Combined sources4
Beta strandi101 – 107Combined sources7
Helixi109 – 112Combined sources4
Beta strandi117 – 120Combined sources4
Helixi128 – 139Combined sources12
Turni140 – 142Combined sources3
Turni146 – 148Combined sources3
Beta strandi149 – 152Combined sources4
Beta strandi155 – 157Combined sources3
Helixi160 – 172Combined sources13
Helixi185 – 193Combined sources9
Helixi200 – 204Combined sources5
Helixi206 – 223Combined sources18
Helixi231 – 248Combined sources18
Turni249 – 251Combined sources3
Helixi255 – 264Combined sources10
Beta strandi269 – 276Combined sources8
Helixi277 – 279Combined sources3
Turni281 – 283Combined sources3
Helixi297 – 303Combined sources7
Helixi307 – 309Combined sources3
Beta strandi313 – 323Combined sources11
Beta strandi325 – 327Combined sources3
Helixi336 – 345Combined sources10
Turni350 – 352Combined sources3
Beta strandi357 – 362Combined sources6
Helixi363 – 373Combined sources11
Beta strandi376 – 381Combined sources6
Helixi383 – 386Combined sources4
Beta strandi390 – 392Combined sources3
Beta strandi397 – 399Combined sources3
Beta strandi401 – 403Combined sources3
Helixi413 – 416Combined sources4
Beta strandi420 – 422Combined sources3
Helixi444 – 457Combined sources14
Beta strandi463 – 465Combined sources3
Beta strandi467 – 471Combined sources5
Beta strandi473 – 475Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DJ3X-ray3.00A/B35-476[»]
ProteinModelPortaliO24396.
SMRiO24396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO24396.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 67IMP bindingUniRule annotation4
Regioni89 – 92IMP bindingUniRule annotation4
Regioni350 – 356Substrate bindingUniRule annotation7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Keywords - Domaini

Transit peptide

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: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

O24396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AAAAAGRGRS FSPAAPAPSS VRLPGRQAPA PAAASALAVE ADPAADRVSS
60 70 80 90 100
LSQVSGVLGS QWGDEGKGKL VDVLAPRFDI VARCQGGANA GHTIYNSEGK
110 120 130 140 150
KFALHLVPSG ILHEGTLCVV GNGAVIHVPG FFGEIDGLQS NGVSCDGRIL
160 170 180 190 200
VSDRAHLLFD LHQTVDGLRE AELANSFIGT TKRGIGPCYS SKVTRNGLRV
210 220 230 240 250
CDLRHMDTFG DKLDVLFEDA AARFEGFKYS KGMLKEEVER YKRFAERLEP
260 270 280 290 300
FIADTVHVLN ESIRQKKKIL VEGGQATMLD IDFGTYPFVT SSSPSAGGIC
310 320 330 340 350
TGLGIAPRVI GDLIGVVKAY TTRVGSGPFP TELLGEEGDV LRKAGMEFGT
360 370 380 390 400
TTGRPRRCGW LDIVALKYCC DINGFSSLNL TKLDVLSGLP EIKLGVSYNQ
410 420 430 440 450
MDGEKLQSFP GDLDTLEQVQ VNYEVLPGWD SDISSVRSYS ELPQAARRYV
460 470
ERIEELAGVP VHYIGVGPGR DALIYK
Length:476
Mass (Da):50,918
Last modified:January 1, 1998 - v1
Checksum:i7E2D9E7F616783DF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49387 mRNA. Translation: AAB16829.1.
PIRiT06792.
UniGeneiTa.121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49387 mRNA. Translation: AAB16829.1.
PIRiT06792.
UniGeneiTa.121.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DJ3X-ray3.00A/B35-476[»]
ProteinModelPortaliO24396.
SMRiO24396.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.
BRENDAi6.3.4.4. 6500.

Miscellaneous databases

EvolutionaryTraceiO24396.

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_WHEAT
AccessioniPrimary (citable) accession number: O24396
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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.