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

Asparagine synthetase, nodule [glutamine-hydrolyzing]

Gene

AS1

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activityBy similarity
Binding sitei98 – 981GlutamineBy similarity
Binding sitei232 – 2321ATP; via carbonyl oxygenBy similarity
Binding sitei268 – 2681ATP; via amide nitrogen and carbonyl oxygenBy similarity
Sitei344 – 3441Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi342 – 3432ATPBy similarity

GO - Molecular functioni

  1. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. glutamine metabolic process Source: UniProtKB-KW
  2. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Asparagine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.

Protein family/group databases

MEROPSiC44.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine synthetase, nodule [glutamine-hydrolyzing] (EC:6.3.5.4)
Alternative name(s):
Glutamine-dependent asparagine synthetase
Gene namesi
Name:AS1
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 586585Asparagine synthetase, nodule [glutamine-hydrolyzing]PRO_0000056926Add
BLAST

Expressioni

Tissue specificityi

Root nodules.

Inductioni

By darkness.

Structurei

3D structure databases

ProteinModelPortaliP19251.
SMRiP19251. Positions 1-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 185184Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini193 – 517325Asparagine synthetaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 545Glutamine bindingBy similarity
Regioni75 – 773Glutamine bindingBy similarity

Sequence similaritiesi

Contains 1 asparagine synthetase domain.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19251-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGILAVLGC SDDSQAKRVR ILELSRRLKH RGPDWSGLHQ HGDNYLAHQR
60 70 80 90 100
LAIVDPASGD QPLFNEDKSI IVTVNGEIYN HEELRKQLPN HKFFTQCDCD
110 120 130 140 150
VIAHLYEEHG ENFVDMLDGI FSFVLLDTRD NSFIVARDAI GVTSLYIGWG
160 170 180 190 200
LDGSVWIASE LKGLNDECEH FEVFPPGHLY SSKEREFRRW YNPPWFNEAI
210 220 230 240 250
IPSTPYDPLV LRNAFEKAVI KRLMTDVPFG VLLSGGLDSS LVASVTARYL
260 270 280 290 300
AGTKAAKQWG AKLPSFCVGL KGAPDLKAGK EVADFLGTVH HEFEFTIQDG
310 320 330 340 350
IDAIEDVIYH TETYDVTTIR AATPMFLMSR KIKSSGVKWV ISGEGSDEIF
360 370 380 390 400
GGYLYFHKAP NREEFHQETC RKIKALHRYD CLRANKSTYA WGLEARVPFL
410 420 430 440 450
DKDFIKVAMD IDPEFKMIKH DEGRIEKWIL RKAFDDEENP YLPKHILYRQ
460 470 480 490 500
KEQFSDGVGY GWIDGIKDHA AKHVTDRMMF NASHIFPFNT PNTKEAYYYR
510 520 530 540 550
MIFERFFPQN SARLTVPGGP SVACSTEKAI EWDASWSNNL DPSGRAALGV
560 570 580
HVSAYEHQIN PVTKGVEPEK IIPKIGVSPL GVAIQT
Length:586
Mass (Da):66,353
Last modified:January 22, 2007 - v3
Checksum:i17C5019A3C8ED491
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52179 mRNA. Translation: CAA36429.1.
Y13321 Genomic DNA. Translation: CAA73762.1.
PIRiS11444. AJPMN1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52179 mRNA. Translation: CAA36429.1.
Y13321 Genomic DNA. Translation: CAA73762.1.
PIRiS11444. AJPMN1.

3D structure databases

ProteinModelPortaliP19251.
SMRiP19251. Positions 1-518.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC44.976.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Dark-induced and organ-specific expression of two asparagine synthetase genes in Pisum sativum."
    Tsai F.Y., Coruzzi G.M.
    EMBO J. 9:323-332(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Sparkle.
    Tissue: Root nodule.
  2. "Light-induced transcriptional repression of the pea AS1 gene: identification of cis-elements and transfactors."
    Ngai N., Tsai F.Y., Coruzzi G.M.
    Plant J. 12:1021-1034(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-84.
    Strain: cv. Feltham First.

Entry informationi

Entry nameiASNS1_PEA
AccessioniPrimary (citable) accession number: P19251
Secondary accession number(s): O49925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1990
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.