Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenylosuccinate synthetase isozyme 2

Gene

ADSS

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. 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 + N6-(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, Adenylosuccinate synthetase isozyme 2 (ADSS), Adenylosuccinate synthetase isozyme 2 (ADSS), Adenylosuccinate synthetase isozyme 1 (ADSSL1), Adenylosuccinate synthetase isozyme 2 (ADSS)
  2. Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, Adenylosuccinate lyase, Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase (ADSL), Adenylosuccinate lyase, 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 sitei40Proton acceptorUniRule annotation1
Metal bindingi40MagnesiumUniRule annotation1
Binding sitei40SubstrateUniRule annotation1
Metal bindingi67Magnesium; via carbonyl oxygenUniRule annotation1
Active sitei68Proton donorUniRule annotation1
Binding sitei162IMPUniRule annotation1
Active sitei173PROSITE-ProRule annotation1
Binding sitei176IMP; shared with dimeric partnerUniRule annotation1
Binding sitei255IMPUniRule annotation1
Binding sitei270IMPUniRule annotation1
Binding sitei334IMPUniRule annotation1
Binding sitei336GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi39 – 45GTPUniRule annotation7
Nucleotide bindingi67 – 69GTPUniRule annotation3
Nucleotide bindingi362 – 364GTPUniRule annotation3
Nucleotide bindingi444 – 447GTPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotation
Biological processPurine biosynthesisUniRule annotation
LigandGTP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00075; UER00335.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetase isozyme 2UniRule annotation (EC:6.3.4.4UniRule annotation)
Short name:
AMPSase 2UniRule annotation
Short name:
AdSS 2UniRule annotation
Alternative name(s):
Adenylosuccinate synthetase, acidic isozymeUniRule annotation
Adenylosuccinate synthetase, liver isozymeUniRule annotation
Short name:
L-type adenylosuccinate synthetaseUniRule annotation
IMP--aspartate ligase 2UniRule annotation
Gene namesi
Name:ADSSUniRule annotationImported
Synonyms:ADSS2UniRule annotation
ORF Names:hCG_15389Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Organism-specific databases

EuPathDBiHostDB:ENSG00000035687.9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

CytoplasmUniRule annotation

PTM / Processingi

Proteomic databases

PaxDbiA0A024R5Q7.
PRIDEiA0A024R5Q7.

Expressioni

Gene expression databases

BgeeiENSG00000035687.
ExpressionAtlasiA0A024R5Q7. baseline and differential.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA0A024R5Q7.
SMRiA0A024R5Q7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 43IMP bindingUniRule annotation4
Regioni65 – 68IMP bindingUniRule annotation4
Regioni330 – 336Substrate bindingUniRule annotation7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG1355. Eukaryota.
COG0104. LUCA.
KOiK01939.
OMAiGIAPFYS.
OrthoDBiEOG091G1BIK.
PhylomeDBiA0A024R5Q7.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
MF_03127. Adenylosucc_synth_vert_acid. 1 hit.
InterProiView protein in InterPro
IPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027529. AdSS_2_vert.
IPR027417. P-loop_NTPase.
PANTHERiPTHR11846. PTHR11846. 1 hit.
PfamiView protein in Pfam
PF00709. Adenylsucc_synt. 1 hit.
SMARTiView protein in SMART
SM00788. Adenylsucc_synt. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00184. purA. 1 hit.
PROSITEiView protein in PROSITE
PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

A0A024R5Q7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL
60 70 80 90 100
AQDADIVCRC QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV
110 120 130 140 150
IHLPGLFEEA EKNVQKGKGL EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ
160 170 180 190 200
RQEQAGKNLG TTKKGIGPVY SSKAARSGLR MCDLVSDFDG FSERFKVLAN
210 220 230 240 250
QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE ALHGPPKKIL
260 270 280 290 300
VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY
310 320 330 340 350
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH
360 370 380 390 400
MINGFTALAL TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV
410 420 430 440 450
QYKTLPGWNT DISNARAFKE LPVNAQNYVR FIEDELQIPV KWIGVGKSRE

SMIQLF
Length:456
Mass (Da):50,097
Last modified:July 9, 2014 - v1
Checksum:i23B7AAC58A238783
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH471148 Genomic DNA. Translation: EAW77103.1.
RefSeqiNP_001117.2. NM_001126.3.
UniGeneiHs.498313.

Genome annotation databases

GeneIDi159.
KEGGihsa:159.

Similar proteinsi

Entry informationi

Entry nameiA0A024R5Q7_HUMAN
AccessioniPrimary (citable) accession number: A0A024R5Q7
Entry historyiIntegrated into UniProtKB/TrEMBL: July 9, 2014
Last sequence update: July 9, 2014
Last modified: September 27, 2017
This is version 29 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.