PUA1C_SALSA
ID PUA1C_SALSA Reviewed; 459 AA.
AC B5DGM4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Adenylosuccinate synthetase isozyme 1 C {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AMPSase 1 C {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AdSS 1 C {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 C {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, muscle isozyme C {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=M-type adenylosuccinate synthetase C {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=IMP--aspartate ligase 1 C {ECO:0000255|HAMAP-Rule:MF_03126};
GN Name=adss1c; Synonyms=adssl1c;
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; BT043783; ACH70898.1; -; mRNA.
DR RefSeq; NP_001133178.1; NM_001139706.1.
DR AlphaFoldDB; B5DGM4; -.
DR SMR; B5DGM4; -.
DR STRING; 8030.ENSSSAP00000036910; -.
DR Ensembl; ENSSSAT00000063751; ENSSSAP00000037902; ENSSSAG00000015427.
DR GeneID; 100194621; -.
DR KEGG; sasa:100194621; -.
DR CTD; 122622; -.
DR OrthoDB; 1276527at2759; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000087266; Chromosome ssa01.
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..459
FT /note="Adenylosuccinate synthetase isozyme 1 C"
FT /id="PRO_0000398890"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT ACT_SITE 73
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 44..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 45..48
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 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 70..73
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 72..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 165
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 179
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 258
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 273
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 333..339
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 337
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 339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 365..367
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 447..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
SQ SEQUENCE 459 AA; 50826 MW; B4F13878AD9CB0AA CRC64;
MSFSWSAKDH KSYTNPPSNP TQGLKRPRND TGNKVTVVLG AQWGDEGKGK VVDLLATESD
LVCRCQGGNN AGHTVVVEGK EYDFHLLPSG IINPKSICVI GNGVVIHLPG LFEEAENNEK
KGLKGWEKRL IVSDRAHLVF DFHQVVDGIQ ETQRQATEGK IIGTTKKGIG PTYASKASRI
GLRVCDLLGD FKEFSTKFKN LVEQYQSMYS SLTVDTESQL KKLKEYGERL RPMVRDGVYY
MYEALHGPPK KILVEGANAA LLDIDFGTYP FVTSSNCTVG GACTGLGIPP LNIGEVYGVS
KAYTTRVGIG AFPTEQLNAT GELLQTRGHE VGVTTGRKRR CGWLDLVILR YAHMINGFTA
IALTKLDILD VLDEIKVGMA YKINGKRIPH FPADMELLHK VEVEYETFPG WKSDTSAARK
WNNLPQKAQN YIRFVESHIG VPIKWVGVGK SRECMIQMF
