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P31752

- ASNS_ASPOF

UniProt

P31752 - ASNS_ASPOF

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Protein

Asparagine synthetase [glutamine-hydrolyzing]

Gene
N/A
Organism
Asparagus officinalis (Garden asparagus)
Status
Reviewed - 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 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

  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 [glutamine-hydrolyzing] (EC:6.3.5.4)
Short name:
AS
OrganismiAsparagus officinalis (Garden asparagus)
Taxonomic identifieri4686 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAsparagaceaeAsparagoideaeAsparagus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 590589Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056920Add
BLAST

Proteomic databases

PRIDEiP31752.

Expressioni

Developmental stagei

Levels of AS increase markedly after harvest.

Structurei

3D structure databases

ProteinModelPortaliP31752.
SMRiP31752. Positions 1-517.
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]
PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
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.

P31752-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCGILAVLGC SDDSQAKRVR VLELSRRLKH RGPDWSGLCQ HGDCFLSHQR
60 70 80 90 100
LAIIDPASGD QPLYNEDKSI VVTVNGEIYN HEELRRRLPD HKYRTGSDCE
110 120 130 140 150
VIAHLYEEHG EDFVDMLDGM FSFVLLDTRN NCFVAARDAV GITPLYIGWG
160 170 180 190 200
LDGSVWLSSE MKGLNDDCEH FEVFPPGNLY SSRSGSFRRW YNPQWYNETI
210 220 230 240 250
PSAPYDPLVL RKAFEDAVIK RLMTDVPFGV LLSGGLDSSL VAAVTARHLA
260 270 280 290 300
GSKAAEQWGT QLHSFCVGLE GSPDLKAAKE VAEYLGTVHH EFHFTVQDGI
310 320 330 340 350
DAIEDVIFHI ETYDVTTIRA STPMFLMARK IKSLGVKMVI SGEGSDEIFG
360 370 380 390 400
GYLYFHKAPN KEEFHHETCR KIKALHQYDC LRANKATSAW GLEARVPFLD
410 420 430 440 450
KEFMDVAMSI DPESKMIKPD LGRIEKWVLR KAFDDEENPY LPKHILYRQK
460 470 480 490 500
EQFSDGVGYS WIDGLKAHAA KHVTDRMMLN AARIYPHNTP TTKEAYYYRM
510 520 530 540 550
IFERFFPQNS ARFTVPGGPS IACSTAKAIE WDARWSNNLD PSGRAALGVH
560 570 580 590
DSAYDPPLPS SISAGKGAAM ITNKKPRIVD VATPGVVIST
Length:590
Mass (Da):66,176
Last modified:January 23, 2007 - v2
Checksum:i9F7CA48BFE0CA712
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti513 – 5131F → L in CAA67889. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67958 mRNA. Translation: CAA48141.1.
X99552 Genomic DNA. Translation: CAA67889.1.
PIRiS25165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67958 mRNA. Translation: CAA48141.1 .
X99552 Genomic DNA. Translation: CAA67889.1 .
PIRi S25165.

3D structure databases

ProteinModelPortali P31752.
SMRi P31752. Positions 1-517.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C44.976.

Proteomic databases

PRIDEi P31752.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00134 ; UER00195 .

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProi IPR006426. 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 ]
Pfami PF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view ]
PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and characterization of a cDNA clone for a harvest-induced asparagine synthetase from Asparagus officinalis L."
    Davies K.M., King G.A.
    Plant Physiol. 102:1337-1340(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Limbras 10.
    Tissue: Spear tip.
  2. "Nucleotide sequence of the asparagine synthetase gene from Asparagus officinalis L."
    Moyle R.L., Davies K.M., King G.A., Farnden K.J.F.
    Plant Gene Register PGR96-096
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiASNS_ASPOF
AccessioniPrimary (citable) accession number: P31752
Secondary accession number(s): Q96231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 1, 2014
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