PURA_BABBO
ID PURA_BABBO Reviewed; 436 AA.
AC A7AU38;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
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=BBOV_II004950;
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo;
RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA Nene V.M.;
RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT hemoprotozoa.";
RL PLoS Pathog. 3:1401-1413(2007).
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; AAXT01000003; EDO06449.1; -; Genomic_DNA.
DR RefSeq; XP_001610017.1; XM_001609967.1.
DR AlphaFoldDB; A7AU38; -.
DR SMR; A7AU38; -.
DR STRING; 5865.XP_001610017.1; -.
DR EnsemblProtists; EDO06449; EDO06449; BBOV_II004950.
DR GeneID; 5478247; -.
DR KEGG; bbo:BBOV_II004950; -.
DR VEuPathDB; PiroplasmaDB:BBOV_II004950; -.
DR eggNOG; KOG1355; Eukaryota.
DR InParanoid; A7AU38; -.
DR OMA; FHHAKPI; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000002173; Partially assembled 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; 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..436
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000399289"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT ACT_SITE 51
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 22..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 23..26
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 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 48..51
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 50..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 141
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 155
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 231
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 246
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 306..312
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 310
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 312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 338..340
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 424..426
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
SQ SEQUENCE 436 AA; 49301 MW; E1A8A908CF6ABD69 CRC64;
MEKTSFSHDT NKVFLIAGMQ WGDEGKGKAV VTFSEKVDIV AKYNGGHNAG HEIILNGQQY
KLHLIPGGVM HPHVINVLGH GMVIHLESLL KEMEILTQHG IEVLERLRIS DRAHILLNAH
VDIDRKMEHR RMSGGGKIGT TLRGIGPCYS TKSARTGIRM GDLLHWEHFS KKVRDFYKIH
CDFENFEELA QEEVENHKKL YDIFAKCICD TGYFMSESIK AGKKILLEGS NGSLLDIDMG
TYPFVTSSTT LACGAYLGLG VPLNAPIYRI GILKCYQTRV GMGPFPTEFF DDNYTHIQKD
GTEIGVSTAR VRRCGWLDLV AARYIQRLNC FNSIYFTKMD VLTGLKEIKI CIDYRNKVDG
TILERGRFPS TIASLEEYEP VYQSFAGWDQ DISQISEYNE LPETARKYIE FVEKEVGAHF
QWVGVGQDVK SIIVRS
