位置:首页 > 蛋白库 > PUA1B_XENLA
PUA1B_XENLA
ID   PUA1B_XENLA             Reviewed;         454 AA.
AC   Q68F20;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Adenylosuccinate synthetase isozyme 1 B {ECO:0000255|HAMAP-Rule:MF_03126};
DE            Short=AMPSase 1 B {ECO:0000255|HAMAP-Rule:MF_03126};
DE            Short=AdSS 1 B {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 B {ECO:0000255|HAMAP-Rule:MF_03126};
DE   AltName: Full=Adenylosuccinate synthetase, muscle isozyme B {ECO:0000255|HAMAP-Rule:MF_03126};
DE            Short=M-type adenylosuccinate synthetase B {ECO:0000255|HAMAP-Rule:MF_03126};
DE   AltName: Full=IMP--aspartate ligase 1 B {ECO:0000255|HAMAP-Rule:MF_03126};
GN   Name=adss1-b; Synonyms=adssl1-b;
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=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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}.
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; BC080025; AAH80025.1; -; mRNA.
DR   RefSeq; NP_001087505.1; NM_001094036.1.
DR   AlphaFoldDB; Q68F20; -.
DR   SMR; Q68F20; -.
DR   DNASU; 447329; -.
DR   GeneID; 447329; -.
DR   KEGG; xla:447329; -.
DR   CTD; 447329; -.
DR   Xenbase; XB-GENE-6254009; adss1.S.
DR   OMA; HIVCDFH; -.
DR   OrthoDB; 1276527at2759; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 447329; Expressed in muscle tissue and 17 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 B"
FT                   /id="PRO_0000398892"
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;  50210 MW;  B34EA4DB3B49C800 CRC64;
     MSGTRASNDR SSHPGAGGHK RPRYDVGNKV TVVLGAQWGD EGKGKVVDLL AMDSDIICRC
     QGGNNAGHTV VVEGKEYDFH LFPSGIINPK AISFIGNGVV IHLPGLFEEA DKNEKKGLKD
     WEKRLIISDR AHIVCDFHQA VDGLQEVQRQ AQEGKNIGTT KKGIGPTYSS KASRTGLRIC
     DLLSDFDEFS ARFKNLAHQY QSMFSNLEVD VDGQLKKLKM YAEKIRPMVR DGVYFMYDAL
     HGSPKKILVE GANAALLDID FGTYPFVTSS NCTVGGVCTG LGIPPQNVGN VYGVVKAYTT
     RVGIGAFPTE QINESGTLLQ TRGHEWGVTT GRKRRCGWLD LVILRYAHMI NGFTALALTK
     LDILDVLDEI KVGVAYRLNG KRIPYFPANQ EILQKIEVEY EVMPGWKSDT TGARKWDDLP
     TKAQNYIRFV ETHIGVPVKW VGVGKSRESM IELF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024