PURA_SCHMA
ID PURA_SCHMA Reviewed; 426 AA.
AC C4QCD2; G4VB95;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03125};
DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_03125};
DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_03125};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03125};
DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_03125};
GN ORFNames=Smp_055990;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=19606141; DOI=10.1038/nature08160;
RA Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P.,
RA Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D.,
RA Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A.,
RA Coulson R., Day T.A., Delcher A., DeMarco R., Djikeng A., Eyre T.,
RA Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y.,
RA Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P.,
RA Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J.,
RA Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M.,
RA Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J.,
RA Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G.,
RA El-Sayed N.M.;
RT "The genome of the blood fluke Schistosoma mansoni.";
RL Nature 460:352-358(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
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 (By similarity).
CC {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_03125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03125};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03125};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03125}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03125}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03125}.
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DR EMBL; HE601624; CCD76606.1; -; Genomic_DNA.
DR RefSeq; XP_018649478.1; XM_018795135.1.
DR AlphaFoldDB; C4QCD2; -.
DR SMR; C4QCD2; -.
DR STRING; 6183.Smp_055990.1; -.
DR GeneID; 8355040; -.
DR KEGG; smm:Smp_055990; -.
DR CTD; 8355040; -.
DR eggNOG; KOG1355; Eukaryota.
DR HOGENOM; CLU_029848_0_0_1; -.
DR InParanoid; C4QCD2; -.
DR OrthoDB; 1276527at2759; -.
DR PhylomeDB; C4QCD2; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000008854; Chromosome 1.
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 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; 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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..426
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000399271"
FT ACT_SITE 19
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT ACT_SITE 47
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 18..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 19..22
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_03125"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 44..47
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_03125"
FT BINDING 46..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 136
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_03125"
FT BINDING 150
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 222
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_03125"
FT BINDING 237
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_03125"
FT BINDING 297..303
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 301
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_03125"
FT BINDING 303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 329..331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 413..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
SQ SEQUENCE 426 AA; 46669 MW; 7B3DCE8768BF3001 CRC64;
MTKSVEGLVS VVLGAQWGDE GKGKLVDLLS ESCSVVCRCQ GGNNAGHTVV AGGQEYFFHL
LPSGIVNPNV LAVIGNGVVV NLQALFQEID EAVCKGLLDV SSRLRISDRC HLVFDIHQEI
DRMEEELRGE NSLGTTKKGI GPTYSSKVTR NGLRVCDLMG DWVQFTAKYK ELVKYVKRRY
PKLGINVEES LEKLSGMVCD SVILINKLVK SKQANILVEG AQSCMLDIDF GTYPHVTSSN
CSVGGVCTGL GLSPSRVGRV YGVIKAYTTR VGSGPFPSEL LDGIGEFIQK KGCEWGVTTK
RKRRIGWLDT VVIRYAHIIN DFNALALTKI DVLDDLEEVK IAKAYIDPET GRELDSFPSD
SSVLNHVVVV YETLPGWKTS THGCRVYEEL PTAAKVFVET VEKLLNIPIR WIGTGASRDS
IIIRSV
