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Protein

Probable asparagine synthetase [glutamine-hydrolyzing]

Gene

MIMI_R475

Organism
Acanthamoeba polyphaga mimivirus (APMV)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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. Probable asparagine synthetase [glutamine-hydrolyzing] (MIMI_R475)
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 sitei100 – 1001GlutamineBy similarity
Binding sitei256 – 2561ATP; via carbonyl oxygenBy similarity
Binding sitei284 – 2841ATP; via amide nitrogen and carbonyl oxygenBy similarity
Sitei362 – 3621Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi360 – 3612ATPBy 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable asparagine synthetase [glutamine-hydrolyzing] (EC:6.3.5.4)
Alternative name(s):
Glutamine-dependent asparagine synthetase
Gene namesi
Ordered Locus Names:MIMI_R475
OrganismiAcanthamoeba polyphaga mimivirus (APMV)
Taxonomic identifieri212035 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageMimiviridaeMimivirus
Virus hostiAcanthamoeba polyphaga (Amoeba) [TaxID: 5757]
ProteomesiUP000001134 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 550549Probable asparagine synthetase [glutamine-hydrolyzing]PRO_0000056930Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ5UQE1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 189188Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini213 – 530318Asparagine synthetaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 575Glutamine bindingBy similarity
Regioni78 – 803Glutamine bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

KOiK01953.

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.

Q5UQE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGIICFIQY GGQKIDLVSC LNCLDKLNNR GPDAQSYQVI ELGDITIFLG
60 70 80 90 100
FTRLAIMDTS EAGLQPFKDN NSNYSICNGE IYNYKNLAEK FNIEMQSQCD
110 120 130 140 150
CEILLPLFNL RGFEGLLSDL DAEFATVIVD KYNSKLYAAR DKYGVRPLYY
160 170 180 190 200
GYNCEKGLIG FASELKALHS VMEYVEQVKP NQYVTIDLSF RPSIPFDLQN
210 220 230 240 250
FVKLFQFTNY HEYYQSHKSL IDYHEPNIEQ LQTSINHLLT EAVRKRLYAD
260 270 280 290 300
RQIGFLLSGG LDSSLIVAIA TRLLGPTNIV CFSVGFEGSP DVAAAREVVK
310 320 330 340 350
FLGIKNHHIV PFSVDIGLNA INDVIKTIET YDITTIRAST PQFIMAKYIQ
360 370 380 390 400
ENTDIRVLLS GEGSDEIHGS YKYMRSAPNS QEFHKETIRL LEELYLFDNK
410 420 430 440 450
RTDRTMAGNG LEVRVPFLDF NYVDFIMNID PNLLMYKSDY IEKKIIRDAF
460 470 480 490 500
KGYLPENILY RPKEAFSDAV SSKEINWYRS IQKITEEIYT DEKLQNSNYK
510 520 530 540 550
FNKPEIKEAL YYRDIFNSHY GGRDHIIPHY WLPRFQQNNV LDPSATILPI
Length:550
Mass (Da):63,335
Last modified:January 23, 2007 - v3
Checksum:i68800D6D26B47778
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY653733 Genomic DNA. Translation: AAV50741.1.
RefSeqiYP_003986982.1. NC_014649.1.

Genome annotation databases

GeneIDi9925100.
KEGGivg:9925100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY653733 Genomic DNA. Translation: AAV50741.1.
RefSeqiYP_003986982.1. NC_014649.1.

3D structure databases

ProteinModelPortaliQ5UQE1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9925100.
KEGGivg:9925100.

Phylogenomic databases

KOiK01953.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Rowbotham-Bradford.

Entry informationi

Entry nameiASNS_MIMIV
AccessioniPrimary (citable) accession number: Q5UQE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 58 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.