位置:首页 > 蛋白库 > PUA2B_XENTR
PUA2B_XENTR
ID   PUA2B_XENTR             Reviewed;         457 AA.
AC   Q28GB0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Adenylosuccinate synthetase isozyme 2 B {ECO:0000255|HAMAP-Rule:MF_03127};
DE            Short=AMPSase 2;
DE            Short=AMPSase 2 B {ECO:0000255|HAMAP-Rule:MF_03127};
DE            Short=AdSS 2 B {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 B {ECO:0000255|HAMAP-Rule:MF_03127};
DE   AltName: Full=Adenylosuccinate synthetase, liver isozyme B {ECO:0000255|HAMAP-Rule:MF_03127};
DE            Short=L-type adenylosuccinate synthetase B {ECO:0000255|HAMAP-Rule:MF_03127};
DE   AltName: Full=IMP--aspartate ligase 2 B {ECO:0000255|HAMAP-Rule:MF_03127};
GN   Name=adss2-b; Synonyms=adss-b; ORFNames=TGas055l19.1;
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=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR761467; CAJ83843.1; -; mRNA.
DR   AlphaFoldDB; Q28GB0; -.
DR   SMR; Q28GB0; -.
DR   InParanoid; Q28GB0; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
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 B"
FT                   /id="PRO_0000398886"
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;  49986 MW;  2D93F81EEA7536A4 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
     LAKLDILDVL SEIKVGVSYK IDGKKIPHFP ANQEVLNRVE VEYETLPGWN TDTCNVRTFE
     ELPENAKKYV RYIELELGIP IKWIGVGKSR ESMIQLF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024