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PURA_THEPA
ID   PURA_THEPA              Reviewed;         434 AA.
AC   Q4N3F4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   OrderedLocusNames=TP04_0033;
OS   Theileria parva (East coast fever infection agent).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5875;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Muguga;
RX   PubMed=15994558; DOI=10.1126/science.1110439;
RA   Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA   Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA   Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA   Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA   Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA   Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA   Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA   Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT   "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT   lymphocytes.";
RL   Science 309:134-137(2005).
CC   -!- FUNCTION: Plays an important role in the salvage pathway for purine
CC       nucleotide biosynthesis. Catalyzes the first committed step in the
CC       biosynthesis of AMP from IMP (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_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   -!- MISCELLANEOUS: Parasitic protozoa lack the de novo purine biosynthesis
CC       pathway and rely exclusively on the salvage pathway for their purine
CC       nucleotide requirements.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03125}.
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DR   EMBL; AAGK01000004; EAN31385.1; -; Genomic_DNA.
DR   RefSeq; XP_763668.1; XM_758575.1.
DR   AlphaFoldDB; Q4N3F4; -.
DR   SMR; Q4N3F4; -.
DR   STRING; 5875.XP_763668.1; -.
DR   EnsemblProtists; EAN31385; EAN31385; TP04_0033.
DR   GeneID; 3500512; -.
DR   KEGG; tpv:TP04_0033; -.
DR   VEuPathDB; PiroplasmaDB:TpMuguga_04g00033; -.
DR   eggNOG; KOG1355; Eukaryota.
DR   InParanoid; Q4N3F4; -.
DR   OMA; FHHAKPI; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000001949; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..434
FT                   /note="Adenylosuccinate synthetase"
FT                   /id="PRO_0000399299"
FT   ACT_SITE        15
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   ACT_SITE        43
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   BINDING         14..20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   BINDING         15..18
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         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
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_03125"
FT   BINDING         42..44
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   BINDING         133
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         147
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         229
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         244
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         304..310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   BINDING         308
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         310
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   BINDING         336..338
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT   BINDING         422..424
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
SQ   SEQUENCE   434 AA;  49035 MW;  4BC0E86FD5D537B6 CRC64;
     MLFQVVLISG MQWGDEGKGK LVSLLSKDFD LVARYNGGHN SGHELFLDGV KYKLHLLPCG
     CLYPNTVNVL GNGVVVHLES LINEIDNLTK LGVDLTNRLF ISERAHLVFD LHIAVDAQLE
     NEQGEHSTSI GTTKRGIGPT NSTKCKRTGI QIGEMLNWDN FEKLLSKLTY KLCHENKVFT
     NSDTRDLLNK QLEQHKVNFS KIADSVVDTS YMIQKYIKEG KKVFFEGANG SLLDLALGTY
     PYVTSSNTTT SGVYNGLGIN PNVKILKVGV LKAYQTRVGK GPFPTELFDE NFNKLQKFGA
     EFGVTTGRVR RCGWLDLVAA KYVQNFSGFD LINLSKLDIL SQFDEIKLCT HYKHKLTGKL
     LEEGRYPSCC YQYDEYEPVY KTMPGWKTDI SKFKTFEELP QNAQNYVLFI EEYLGVFIYW
     IGTGRDVNSM IVRT
 
 
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