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Protein

Asparagine synthetase [glutamine-hydrolyzing] 1

Gene

AS1

Organism
Lotus japonicus (Lotus corniculatus var. japonicus)
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.

Pathway: L-asparagine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route).
Proteins known to be involved in this subpathway in this organism are:
  1. Asparagine synthetase [glutamine-hydrolyzing] 2 (AS2), Asparagine synthetase [glutamine-hydrolyzing] 1 (AS1)
This subpathway is part of the pathway L-asparagine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route), the pathway L-asparagine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activityBy similarity
Binding sitei98 – 981GlutamineBy similarity
Binding sitei231 – 2311ATP; via carbonyl oxygenBy similarity
Binding sitei267 – 2671ATP; via amide nitrogen and carbonyl oxygenBy similarity
Sitei343 – 3431Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi341 – 3422ATPBy similarity

GO - Molecular functioni

GO - Biological processi

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 [glutamine-hydrolyzing] 1 (EC:6.3.5.4)
Alternative name(s):
Glutamine-dependent asparagine synthetase 1
Gene namesi
Name:AS1
OrganismiLotus japonicus (Lotus corniculatus var. japonicus)
Taxonomic identifieri34305 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeLoteaeLotus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 586585Asparagine synthetase [glutamine-hydrolyzing] 1PRO_0000056922Add
BLAST

Proteomic databases

ProMEXiP49092.

Structurei

3D structure databases

ProteinModelPortaliP49092.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 185184Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini193 – 516324Asparagine 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.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. 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.
TIGRFAMsiTIGR01536. asn_synth_AEB. 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.

P49092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGILAVLGC SDFTQAKRVR VLELSRRLKH RGPDWSGLHQ HGDCYLAHQR
60 70 80 90 100
LAIVDPASGD QPLFNEDKSI IVTVNGEIYN HEELRKQLPN HQFRTGSDCD
110 120 130 140 150
VIAHLYEEHG ENFMDMLDGI FSFVLLDTRD NTFIVARDAI GVTSLYIGWG
160 170 180 190 200
LDGSVWISSE MKGLNDDCEH FEVFPPGHLY SSRERAFRRW YNPTWFSESI
210 220 230 240 250
PSAPYDPLAV RHAFEKAVIK RLMTDVPFGV LLSGGLDSSL VASITSRYLA
260 270 280 290 300
TTKAAEQWGS KLHSFCVGLE GSPDLKAAKE VADYLGTVHH EFTFTVQDGI
310 320 330 340 350
DAIEEVIYHV ETYDVTTIRA STPMFLMSRK IKSLGVKWVI SGEGSDEIFG
360 370 380 390 400
GYLYFHKAPN KEEFHTETCR KIKALHQYDC LRANKSTFAW GLEARVPFLD
410 420 430 440 450
KEFINVAMNI DPEYKMIKRD EGRIEKYILR RAFDDEEKPY LPKHILYRQK
460 470 480 490 500
EQFSDGVGYS WIDGLKDHAA KHVTDKMILN AGNIFRHNTP LTKEAYYYRM
510 520 530 540 550
IFERFFPQNS ARLTVPGGPT VACSTAKAVE WDAAWSNNLD PSGRAALGVH
560 570 580
LSAYDDKQNN LINNKPVEFE KLIPMEAPSL GVAIHS
Length:586
Mass (Da):66,461
Last modified:January 23, 2007 - v2
Checksum:iAD32149B6A70CEEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89409 mRNA. Translation: CAA61589.1.
PIRiS69182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89409 mRNA. Translation: CAA61589.1.
PIRiS69182.

3D structure databases

ProteinModelPortaliP49092.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC44.976.

Proteomic databases

ProMEXiP49092.

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.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. 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.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and characterisation of asparagine synthetase from Lotus japonicus: dynamics of asparagine synthesis in N-sufficient conditions."
    Waterhouse R.N., Smyth A.J., Massoneau A., Prosser I.M., Clarkson D.T.
    Plant Mol. Biol. 30:883-897(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Gifu / B-129.

Entry informationi

Entry nameiASNS1_LOTJA
AccessioniPrimary (citable) accession number: P49092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 82 of the entry and version 2 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.