Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 (PURA), Adenylosuccinate synthetase, chloroplastic (PURA), Adenylosuccinate synthetase, chloroplastic, Adenylosuccinate synthetase, chloroplastic (PURA), Adenylosuccinate synthetase, chloroplastic (PURA), Adenylosuccinate synthetase, chloroplastic (PURA), 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Proton acceptorUniRule annotation
Metal bindingi64 – 641MagnesiumUniRule annotation
Metal bindingi91 – 911Magnesium; via carbonyl oxygenUniRule annotation
Active sitei92 – 921Proton donorUniRule annotation
Binding sitei181 – 1811IMPUniRule annotation
Binding sitei195 – 1951IMP; shared with dimeric partnerUniRule annotation
Binding sitei275 – 2751IMPUniRule annotation
Binding sitei290 – 2901IMPUniRule annotation
Binding sitei354 – 3541IMPUniRule annotation
Binding sitei356 – 3561GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi63 – 697GTP
Nucleotide bindingi91 – 933GTP
Nucleotide bindingi382 – 3843GTP
Nucleotide bindingi465 – 4673GTP

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 476Adenylosuccinate synthetase, chloroplasticPRO_0000029872
Transit peptidei‹1 – ?Chloroplast

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 493Combined sources
Beta strandi53 – 597Combined sources
Beta strandi61 – 633Combined sources
Helixi67 – 748Combined sources
Helixi75 – 773Combined sources
Beta strandi79 – 835Combined sources
Beta strandi92 – 954Combined sources
Beta strandi101 – 1077Combined sources
Helixi109 – 1124Combined sources
Beta strandi117 – 1204Combined sources
Helixi128 – 13912Combined sources
Turni140 – 1423Combined sources
Turni146 – 1483Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi155 – 1573Combined sources
Helixi160 – 17213Combined sources
Helixi185 – 1939Combined sources
Helixi200 – 2045Combined sources
Helixi206 – 22318Combined sources
Helixi231 – 24818Combined sources
Turni249 – 2513Combined sources
Helixi255 – 26410Combined sources
Beta strandi269 – 2768Combined sources
Helixi277 – 2793Combined sources
Turni281 – 2833Combined sources
Helixi297 – 3037Combined sources
Helixi307 – 3093Combined sources
Beta strandi313 – 32311Combined sources
Beta strandi325 – 3273Combined sources
Helixi336 – 34510Combined sources
Turni350 – 3523Combined sources
Beta strandi357 – 3626Combined sources
Helixi363 – 37311Combined sources
Beta strandi376 – 3816Combined sources
Helixi383 – 3864Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi397 – 3993Combined sources
Beta strandi401 – 4033Combined sources
Helixi413 – 4164Combined sources
Beta strandi420 – 4223Combined sources
Helixi444 – 45714Combined sources
Beta strandi463 – 4653Combined sources
Beta strandi467 – 4715Combined sources
Beta strandi473 – 4753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJ3X-ray3.00A/B35-476[»]
ProteinModelPortaliO24396.
SMRiO24396. Positions 45-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO24396.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 674IMP bindingUniRule annotation
Regioni89 – 924IMP bindingUniRule annotation
Regioni350 – 3567Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Keywords - Domaini

Transit peptide

Family and domain databases

HAMAPiMF_00011. Adenylosucc_synth.
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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJ3X-ray3.00A/B35-476[»]
ProteinModelPortaliO24396.
SMRiO24396. Positions 45-476.
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

HAMAPiMF_00011. Adenylosucc_synth.
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...

Publicationsi

  1. "The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase."
    Fonne-Pfister R., Chemla P., Ward E., Girardet M., Kreuz K.E., Honzatko R.B., Fromm H.J., Schaer H.-P., Gruetter M.G., Cowan-Jacob S.W.
    Proc. Natl. Acad. Sci. U.S.A. 93:9431-9436(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Kanzler.
  2. "Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana."
    Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R.
    J. Mol. Biol. 296:569-577(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-476 IN COMPLEX WITH GDP.

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: April 13, 2016
This is version 104 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.