PUA1A_XENLA
ID PUA1A_XENLA Reviewed; 454 AA.
AC Q561L1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Adenylosuccinate synthetase isozyme 1 A {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AMPSase 1 A {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AdSS 1 A {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 A {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, muscle isozyme A {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=M-type adenylosuccinate synthetase A {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=IMP--aspartate ligase 1 A {ECO:0000255|HAMAP-Rule:MF_03126};
GN Name=adss1-a; Synonyms=adssl1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03126}.
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DR EMBL; BC093568; AAH93568.1; -; mRNA.
DR RefSeq; NP_001090012.1; NM_001096543.1.
DR AlphaFoldDB; Q561L1; -.
DR SMR; Q561L1; -.
DR PRIDE; Q561L1; -.
DR DNASU; 735084; -.
DR GeneID; 735084; -.
DR KEGG; xla:735084; -.
DR CTD; 735084; -.
DR Xenbase; XB-GENE-5758296; adss1.L.
DR OMA; RYAHMLN; -.
DR OrthoDB; 1276527at2759; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 735084; Expressed in muscle tissue and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..454
FT /note="Adenylosuccinate synthetase isozyme 1 A"
FT /id="PRO_0000398891"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT ACT_SITE 68
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 39..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 40..43
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 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 65..68
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 67..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 160
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 174
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 253
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 268
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 328..334
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 332
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 334
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 360..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 442..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
SQ SEQUENCE 454 AA; 50354 MW; 119319E6A5582D13 CRC64;
MSGTRASNDR SSHPGAGGHK RPRYDVGNKV TVILGAQWGD EGKGKVVDLL ATDSDIICRC
QGGNNAGHTV VVEGKEYDFH LFPSGIINPK AISFIGNGVV IHLPGLFEEA DKNEKKGLKD
WEKRLIISDR AHIVFDFHQA VDGLQEVQRQ AQEGKNIGTT KKGIGPTYSS KASRTGLRIC
DLLSDFDEFS ARFKNLAHQH QSMFSNLEVD VEGQLKKLKM YAEKIRPMVR DGVYFMYEAL
HGSPKKILVE GANAALLDID FGTYPFVTSS NCTVGGVCTG LGIPPQNVGD VYGVVKAYTT
RVGIGAFPTE QINEIGNILQ TRGHEWGVTT GRKRRCGWLD LVILRYAHMI NGFTALALTK
LDILDVLDEM KIGVAYRLNG KRIPYFPANQ EILQKVEVEY EVMPGWKSDT TGARKWEDLP
TRAQNYIRFV ENHIGVPVKW VGVGKSRESM IELF
