PUA1B_SALSA
ID PUA1B_SALSA Reviewed; 449 AA.
AC B5DGM3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=adss1b; Synonyms=adssl1b;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=White muscle;
RX PubMed=19878547; DOI=10.1186/1471-2164-10-502;
RA Andreassen R., Lunner S., Hoyheim B.;
RT "Characterization of full-length sequenced cDNA inserts (FLIcs) from
RT Atlantic salmon (Salmo salar).";
RL BMC Genomics 10:502-502(2009).
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 (By similarity). {ECO:0000250}.
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; BT043782; ACH70897.1; -; mRNA.
DR RefSeq; NP_001133177.1; NM_001139705.1.
DR AlphaFoldDB; B5DGM3; -.
DR SMR; B5DGM3; -.
DR STRING; 8030.ENSSSAP00000006372; -.
DR GeneID; 100194620; -.
DR KEGG; sasa:100194620; -.
DR CTD; 11565; -.
DR OMA; RYAHMLN; -.
DR OrthoDB; 1276527at2759; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000087266; Chromosome ssa06.
DR Bgee; ENSSSAG00000003104; Expressed in muscle tissue and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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_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..449
FT /note="Adenylosuccinate synthetase isozyme 1 B"
FT /id="PRO_0000398889"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 35..38
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 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 60..63
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 62..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 155
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 169
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 248
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 263
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 323..329
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 327
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 329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 355..357
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 437..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
SQ SEQUENCE 449 AA; 49652 MW; 788226D3C43ED9D3 CRC64;
MSHKACYTNP GAGVKRPRND TGNKLTVVLG AQWGDEGKGK VVDLLATESD IICRCQGGNN
AGHTVVVDGK EYDFHLLPSG IINSKALSVI GNGVVIHLPG LFEEAEKNEK NGLKDWEKRL
IISDRAHIVF DFHQAVDGLQ EVQRQAQEGK NIGTTKKGIG PTYSSKASRT GLRICDLLAD
FKDFSMRFKN LAQQYQAMFP TLEVDVDGQL KKLKEYAERI RPMVRDGVYF MYDAINGPPK
KILVEGANAA LLDIDFGTYP FVTSSNCTVG GVCTGLGIPP LNIGDVYGVV KAYTTRVGIG
AFPTEQLNEV GELLQTRGHE VGVTTGRKRR CGWLDLVILR YANMINGFTA FALTKLDILD
VMDEIKVGVS YKLNGKKIPY FPANMDVLQK VEVEYEKLPG WKSDTSACRK WEDLPVKAQN
YIRFVEIHVG VPIKWVGVGK ARESMIQMF
