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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei43 – 431Proton acceptorUniRule annotation
Metal bindingi43 – 431MagnesiumUniRule annotation
Binding sitei43 – 431SubstrateUniRule annotation
Metal bindingi70 – 701Magnesium; via carbonyl oxygenUniRule annotation
Active sitei71 – 711Proton donorUniRule annotation
Binding sitei163 – 1631IMPUniRule annotation
Binding sitei177 – 1771IMP; shared with dimeric partnerUniRule annotation
Binding sitei256 – 2561IMPUniRule annotation
Binding sitei271 – 2711IMPUniRule annotation
Binding sitei335 – 3351IMPUniRule annotation
Binding sitei337 – 3371GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 487GTPUniRule annotation
Nucleotide bindingi70 – 723GTPUniRule annotation
Nucleotide bindingi363 – 3653GTPUniRule annotation
Nucleotide bindingi445 – 4484GTPUniRule annotation

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

ExpressionAtlasiQ3UBP0. baseline and differential.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021726.

Structurei

3D structure databases

SMRiQ3UBP0. Positions 27-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 464IMP bindingUniRule annotation
Regioni68 – 714IMP bindingUniRule annotation
Regioni331 – 3377Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG1355. Eukaryota.
COG0104. LUCA.
GeneTreeiENSGT00390000015553.
HOVERGENiHBG053768.
KOiK01939.
PhylomeDBiQ3UBP0.

Family and domain databases

HAMAPiMF_00011. Adenylosucc_synth.
MF_03126. Adenylosucc_synth_vert_basic.
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

SMRiQ3UBP0. Positions 27-457.
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.
GeneTreeiENSGT00390000015553.
HOVERGENiHBG053768.
KOiK01939.
PhylomeDBiQ3UBP0.

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.

Miscellaneous databases

ChiTaRSiAdssl1. mouse.
NextBioi279066.
SOURCEiSearch...

Gene expression databases

ExpressionAtlasiQ3UBP0. baseline and differential.

Family and domain databases

HAMAPiMF_00011. Adenylosucc_synth.
MF_03126. Adenylosucc_synth_vert_basic.
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...

Publicationsi

  1. "High-efficiency full-length cDNA cloning."
    Carninci P., Hayashizaki Y.
    Methods Enzymol. 303:19-44(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  2. "Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes."
    Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.
    Genome Res. 10:1617-1630(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  5. "Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs."
    The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team
    Nature 420:563-573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  6. "A comparison of whole-genome shotgun-derived mouse chromosome 16 and the human genome."
    Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.
    , Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.
    Science 296:1661-1671(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  7. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  8. "The Transcriptional Landscape of the Mammalian Genome."
    The FANTOM Consortium, Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group)
    Science 309:1559-1563(2005)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  9. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Bone marrowImported and HeartImported.
  10. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.

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: May 11, 2016
This is version 98 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.