PURA2_XENLA
ID PURA2_XENLA Reviewed; 457 AA.
AC Q7ZY87;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Adenylosuccinate synthetase isozyme 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AMPSase 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AdSS 2 {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 {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, liver isozyme {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=L-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=IMP--aspartate ligase 2 {ECO:0000255|HAMAP-Rule:MF_03127};
GN Name=adss2; Synonyms=adss;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-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; BC043896; AAH43896.1; -; mRNA.
DR RefSeq; NP_001080088.1; NM_001086619.1.
DR RefSeq; XP_018097984.1; XM_018242495.1.
DR AlphaFoldDB; Q7ZY87; -.
DR SMR; Q7ZY87; -.
DR DNASU; 379780; -.
DR GeneID; 379780; -.
DR KEGG; xla:379780; -.
DR CTD; 379780; -.
DR Xenbase; XB-GENE-944129; adss2.L.
DR OrthoDB; 1276527at2759; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 108705604; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
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_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"
FT /id="PRO_0000398885"
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; 50080 MW; FB8C29B2FC73BF69 CRC64;
MSAENESPGL PNGGACCASA TGHFLLVGNK VTVVLGAQWG DEGKGKVVDL LAQDADIVCR
CQGGNNAGHT VVVDSVEYDF HLLPSGIINQ NAIAFIGNGV VIHLPGLFEE AEKNLKKGQG
LAGWEKRLCI SDRAHIVFDF HQAADGIQEQ QRQEQAGKNL GTTKKGIGPV YSSKAARSGL
RMCDLVSDFN EFSQRFKLLA KQYKSMYPSL EIDIDGELKK LQDYADRVKP MVKDGVYYIY
EALHGPPKKI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQS IGDVYGVVKA
YTTRVGIGAF PTEQNNDIGE MLQTRGHEYG VTTGRKRRCG WLDLVLLRYA HMINGFTALA
LTKLDILDVF SEIKVGVSYK IDGKNIPHFP ANQEVLNKVE VEYETLPGWN KDTSNVRTFE
ELPENAKKYV QFIKEELGIP IKWIGVGKSR ESMIQLF
