PUA2A_XENTR
ID PUA2A_XENTR Reviewed; 457 AA.
AC Q6P875;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Adenylosuccinate synthetase isozyme 2 A {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AMPSase 2;
DE Short=AMPSase 2 A {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AdSS 2 A {ECO:0000255|HAMAP-Rule:MF_03127};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, acidic isozyme A {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, liver isozyme A {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=L-type adenylosuccinate synthetase A {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=IMP--aspartate ligase 2 A {ECO:0000255|HAMAP-Rule:MF_03127};
GN Name=adss2-a; Synonyms=adss-a;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the de novo pathway and in the
CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first
CC committed step in the biosynthesis of AMP from IMP.
CC {ECO:0000250|UniProtKB:P46664}.
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_03127};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03127};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03127};
CC -!- ACTIVITY REGULATION: Inhibited competitively by AMP and IMP and non-
CC competitively by fructose 1,6-bisphosphate.
CC {ECO:0000250|UniProtKB:P46664}.
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03127}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03127}.
CC Mitochondrion {ECO:0000250|UniProtKB:A4Z6H1}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03127}.
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DR EMBL; BC061354; AAH61354.1; -; mRNA.
DR RefSeq; NP_989047.1; NM_203716.1.
DR AlphaFoldDB; Q6P875; -.
DR SMR; Q6P875; -.
DR STRING; 8364.ENSXETP00000060819; -.
DR PaxDb; Q6P875; -.
DR DNASU; 394644; -.
DR GeneID; 394644; -.
DR KEGG; xtr:394644; -.
DR CTD; 159; -.
DR Xenbase; XB-GENE-944123; adss2.
DR eggNOG; KOG1355; Eukaryota.
DR InParanoid; Q6P875; -.
DR OrthoDB; 1276527at2759; -.
DR Reactome; R-XTR-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014538; Expressed in egg cell and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central.
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 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_03127; Adenylosucc_synth_vert_acid; 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; IPR027529; AdSS_2_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; Mitochondrion;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..457
FT /note="Adenylosuccinate synthetase isozyme 2 A"
FT /id="PRO_0000398883"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 40..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 41..44
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_03127"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 66..69
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_03127"
FT BINDING 68..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 163
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_03127"
FT BINDING 177
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 256
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_03127"
FT BINDING 271
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_03127"
FT BINDING 331..337
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 335
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_03127"
FT BINDING 337
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 363..365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 445..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
SQ SEQUENCE 457 AA; 50016 MW; 46FE4EC587DE46B0 CRC64;
MSAENGSPGL PNGGVCCATD SGRCSLVGNK VTVVLGAQWG DEGKGKVVDL LAQDADIVCR
CQGGNNAGHT VVVDSVEYDF HLLPSGIINQ NAIAFIGNGV VIHLPGLFEE AEKNLKKGQG
LVGWEKRLCI SDRAHIVFDF HQAADGIQEQ QRQEQAGKNL GTTKKGIGPV YSSKAARSGL
RMCDLVSDFS EFSQRFKLLA KQYKSMYPSL EIDIDGELKK LQDYADRVKP MVKDGVYYLY
EALHGPPKNI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQS VGDVYGVVKA
YTTRVGIGAF PTEQNNDTGE MLQTRGHEYG VTTGRKRRCG WLDLVLLRYA HMINGFTALA
LTKLDILDVL SEIKVGVSYK IDGKKIPHFP ANQEVLNRVE VEYETLPGWN TDTCNVRTFE
ELPENAKKYV RYIELELGIP IKWIGVGKSR ESMIQLF
