PURA1_DANRE
ID PURA1_DANRE Reviewed; 456 AA.
AC Q6NSN5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Adenylosuccinate synthetase isozyme 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AMPSase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AdSS 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, basic isozyme {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, muscle isozyme {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=M-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=IMP--aspartate ligase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
GN Name=adss1; Synonyms=adssl1; ORFNames=zgc:85738;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=26506222; DOI=10.1002/ana.24550;
RA Park H.J., Hong Y.B., Choi Y.C., Lee J., Kim E.J., Lee J.S., Mo W.M.,
RA Ki S.M., Kim H.I., Kim H.J., Hyun Y.S., Hong H.D., Nam K., Jung S.C.,
RA Kim S.B., Kim S.H., Kim D.H., Oh K.W., Kim S.H., Yoo J.H., Lee J.E.,
RA Chung K.W., Choi B.O.;
RT "ADSSL1 mutation relevant to autosomal recessive adolescent onset distal
RT myopathy.";
RL Ann. Neurol. 79:231-243(2016).
CC -!- FUNCTION: Component of the purine nucleotide cycle (PNC), which
CC interconverts IMP and AMP to regulate the nucleotide levels in various
CC tissues, and which contributes to glycolysis and ammoniagenesis.
CC Catalyzes the first committed step in the biosynthesis of AMP from IMP.
CC {ECO:0000250|UniProtKB:Q8N142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03126};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03126};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03126};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03126}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03126}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein in embryos
CC results in severe disruption of muscle fibers.
CC {ECO:0000269|PubMed:26506222}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03126}.
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DR EMBL; BC070009; AAH70009.1; -; mRNA.
DR RefSeq; NP_999985.1; NM_214820.1.
DR AlphaFoldDB; Q6NSN5; -.
DR SMR; Q6NSN5; -.
DR STRING; 7955.ENSDARP00000046076; -.
DR iPTMnet; Q6NSN5; -.
DR PaxDb; Q6NSN5; -.
DR Ensembl; ENSDART00000172540; ENSDARP00000136105; ENSDARG00000099517.
DR GeneID; 407989; -.
DR KEGG; dre:407989; -.
DR CTD; 122622; -.
DR ZFIN; ZDB-GENE-040516-18; adss1.
DR eggNOG; KOG1355; Eukaryota.
DR GeneTree; ENSGT00390000015553; -.
DR InParanoid; Q6NSN5; -.
DR OMA; HKNTNQP; -.
DR OrthoDB; 1276527at2759; -.
DR PhylomeDB; Q6NSN5; -.
DR TreeFam; TF300486; -.
DR Reactome; R-DRE-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00075; UER00335.
DR PRO; PR:Q6NSN5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000099517; Expressed in muscle tissue and 20 other tissues.
DR ExpressionAtlas; Q6NSN5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:ZFIN.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:ZFIN.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR Gene3D; 3.90.170.10; -; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR HAMAP; MF_03126; Adenylosucc_synth_vert_basic; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027509; AdSS_1_vert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00184; purA; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..456
FT /note="Adenylosuccinate synthetase isozyme 1"
FT /id="PRO_0000398887"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT ACT_SITE 70
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 41..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 42..45
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 67..70
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 69..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 162
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 176
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 255
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 270
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 330..336
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 334
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 336
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 362..364
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 444..447
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 456 AA; 50374 MW; 800011BE05689071 CRC64;
MSSGWSQNDH RSYSNPPPVS GKRPRNDSGN KVTVVLGAQW GDEGKGKVVD LLATESDIVG
RCQGGNNAGH TVVVEEKEYD FHLLPSGIIN TKCTSFIGNG VVIHLPGLFE EIDKNEKKGL
KGWEKRLVIS DRAHIVFDFH QAVDGLQETQ RQAQEGKNIG TTKKGIGPTY ACKASRTGLR
ICDLMADFNE FSTRVKNLVQ QYQSMYPTLK VDVESELKKL KEYAERIRPL VRDGVYFMYD
AIHGPQKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGIPPANI GDVYGVSKAY
TTRVGIGAFP TEQLNAVGEL LQTRGHEVGV TTGRKRRCGW LDLVILKYAH MINGFTAIAL
TKLDILDVLD EIKVGVAYKI NGKRIPHFPA NLEVLQKVEV EYETFPGWKS DTSAARKWGD
LPAKAQNYIR FVENHIGVPI KWVGVGKSRE CMIQMF
