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Protein

Adenylosuccinate synthetase isozyme 1

Gene

Adssl1

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.UniRule annotation
Plays an important role in the de novo pathway of purine nucleotide biosynthesis.UniRule annotation

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 isozyme 1 (Adssl1), Adenylosuccinate synthetase isozyme 1 (Adssl1), Adenylosuccinate synthetase (Adss), Adenylosuccinate synthetase isozyme 2 (Adss), Adenylosuccinate synthetase isozyme 2 (Adss), Adenylosuccinate synthetase isozyme 1 (Adssl1)
  2. Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl)
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)DescriptionActionsGraphical viewLength
Active sitei43Proton acceptorUniRule annotation1
Metal bindingi43MagnesiumUniRule annotation1
Binding sitei43SubstrateUniRule annotation1
Metal bindingi70Magnesium; via carbonyl oxygenUniRule annotation1
Active sitei71Proton donorUniRule annotation1
Binding sitei163IMPUniRule annotation1
Binding sitei177IMP; shared with dimeric partnerUniRule annotation1
Binding sitei256IMPUniRule annotation1
Binding sitei271IMPUniRule annotation1
Binding sitei335IMPUniRule annotation1
Binding sitei337GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 48GTPUniRule annotation7
Nucleotide bindingi70 – 72GTPUniRule annotation3
Nucleotide bindingi363 – 365GTPUniRule annotation3
Nucleotide bindingi445 – 448GTPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Keywords - Ligandi

GTP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetase isozyme 1UniRule annotation (EC:6.3.4.4UniRule annotation)
Short name:
AMPSase 1UniRule annotation
Short name:
AdSS 1UniRule annotation
Alternative name(s):
Adenylosuccinate synthetase, basic isozymeUniRule annotation
Adenylosuccinate synthetase, muscle isozymeUniRule annotation
IMP--aspartate ligase 1UniRule annotation
Gene namesi
Name:Adssl1UniRule annotationImported
Synonyms:Adss1UniRule annotation
ORF Names:mCG_15400Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Organism-specific databases

MGIiMGI:87947. Adssl1.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Expressioni

Gene expression databases

BgeeiENSMUSG00000011148.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021726.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 46IMP bindingUniRule annotation4
Regioni68 – 71IMP bindingUniRule annotation4
Regioni331 – 337Substrate bindingUniRule annotation7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG1355. Eukaryota.
COG0104. LUCA.
HOVERGENiHBG053768.
KOiK01939.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
MF_03126. Adenylosucc_synth_vert_basic. 1 hit.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027509. AdSS_1_vert.
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: Complete.

Q3UBP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV
60 70 80 90 100
DLLATDADIV SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN
110 120 130 140 150
GVVIHLPGLF EEAEKNEKKG LKDWEKRLII SDRAHLVFDF HQAVDGLQEV
160 170 180 190 200
QRQAQEGKNI GTTKKGIGPT YSSKAARTGL RICDLLSDFD EFSARFKNLA
210 220 230 240 250
HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY EALHGPPKKV
260 270 280 290 300
LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA
310 320 330 340 350
YTTRVGIGAF PTEQINEIGD LLQNRGHEWG VTTGRKRRCG WLDLMILRYA
360 370 380 390 400
HMVNGFTALA LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE
410 420 430 440 450
VEYETLPGWK ADTTGARKWE DLPPQAQSYV RFVENHMGVA VKWVGVGKSR

ESMIQLF
Length:457
Mass (Da):50,254
Last modified:October 11, 2005 - v1
Checksum:iEBEC85BF907B7FED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146907 mRNA. Translation: BAE27520.1.
AK150874 mRNA. Translation: BAE29924.1.
CH466549 Genomic DNA. Translation: EDL18590.1.
RefSeqiNP_031447.1. NM_007421.2.
UniGeneiMm.3440.

Genome annotation databases

GeneIDi11565.
KEGGimmu:11565.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146907 mRNA. Translation: BAE27520.1.
AK150874 mRNA. Translation: BAE29924.1.
CH466549 Genomic DNA. Translation: EDL18590.1.
RefSeqiNP_031447.1. NM_007421.2.
UniGeneiMm.3440.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021726.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11565.
KEGGimmu:11565.

Organism-specific databases

CTDi122622.
MGIiMGI:87947. Adssl1.

Phylogenomic databases

eggNOGiKOG1355. Eukaryota.
COG0104. LUCA.
HOVERGENiHBG053768.
KOiK01939.

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.

Miscellaneous databases

ChiTaRSiAdssl1. mouse.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000011148.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
MF_03126. Adenylosucc_synth_vert_basic. 1 hit.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027509. AdSS_1_vert.
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...

Entry informationi

Entry nameiQ3UBP0_MOUSE
AccessioniPrimary (citable) accession number: Q3UBP0
Entry historyi
Integrated into UniProtKB/TrEMBL: October 11, 2005
Last sequence update: October 11, 2005
Last modified: November 30, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.