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PURA_MYCCT
ID   PURA_MYCCT              Reviewed;         432 AA.
AC   Q2SR96;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011};
DE            Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011};
DE            Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011};
DE            EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011};
DE   AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011};
GN   Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; OrderedLocusNames=MCAP_0767;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis. Catalyzes the first committed step in the
CC       biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
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_00011};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00011};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00011}.
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DR   EMBL; CP000123; ABC01501.1; -; Genomic_DNA.
DR   RefSeq; WP_011387601.1; NC_007633.1.
DR   AlphaFoldDB; Q2SR96; -.
DR   SMR; Q2SR96; -.
DR   EnsemblBacteria; ABC01501; ABC01501; MCAP_0767.
DR   GeneID; 23778281; -.
DR   KEGG; mcp:MCAP_0767; -.
DR   HOGENOM; CLU_029848_0_0_14; -.
DR   OMA; FHHAKPI; -.
DR   OrthoDB; 232152at2; -.
DR   PhylomeDB; Q2SR96; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000001928; Chromosome.
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.
FT   CHAIN           1..432
FT                   /note="Adenylosuccinate synthetase"
FT                   /id="PRO_1000000867"
FT   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   ACT_SITE        45
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         16..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         17..20
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_00011"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         42..45
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_00011"
FT   BINDING         44..46
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         132
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_00011"
FT   BINDING         146
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         226
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_00011"
FT   BINDING         241
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_00011"
FT   BINDING         301..307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         305
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_00011"
FT   BINDING         307
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         333..335
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         415..417
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
SQ   SEQUENCE   432 AA;  48943 MW;  14506B07DCA7E715 CRC64;
     MKNNYKSLVI VGSQWGDEGK GKITDYFSQK ADAVVRFAGG DNAGHMIEFN NKRHKVTIIP
     SGVFNPKVKN IIGNGTVINL KSLVNEIKRL NESNISTDNV YISDRAHLIF DWHTLIDQLQ
     EENRKENKIG TTKRGIGPSY ADKAARYGIR ICDLKSPNFK EIFKENLDYH NEIITKVYNH
     KPLDFDQIYN ELLTNYQLIK NNIIDCGYEV SNLINENKFV LFEGAQGVLL DIDHGTYPFV
     TSSNCSANNA SIGTGIHAKQ IQKVIGIVKA YNTRVGSGAM PTEIKTELAN KLRERGREYG
     SNTGKPRRIG WLDLVALKYA IRVGGIDQLF LTLFDVLDTE EKIKICTAYK LDNQIIHSIP
     ANENDFKRCE PIYEELDGWN EDITKITSFE QLPINAQNYI KRIQEIVNVP FLGFSVGPDR
     KQTILIKGEF DD
 
 
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