(data stored in ACNUC7421 zone)

SWISSPROT: PURA_FRASN

ID   PURA_FRASN              Reviewed;         427 AA.
AC   A8LDR3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 72.
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};
GN   OrderedLocusNames=Franean1_0211;
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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-
CC       Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP 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}.
DR   EMBL; CP000820; ABW09678.1; -; Genomic_DNA.
DR   RefSeq; WP_012157655.1; NC_009921.1.
DR   SMR; A8LDR3; -.
DR   STRING; 298653.Franean1_0211; -.
DR   EnsemblBacteria; ABW09678; ABW09678; Franean1_0211.
DR   KEGG; fre:Franean1_0211; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; SNAGHTV; -.
DR   OrthoDB; 232152at2; -.
DR   BioCyc; FSP298653:G1G9X-205-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000001313; 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;
DR   PRODOM; A8LDR3.
DR   SWISS-2DPAGE; A8LDR3.
KW   Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    427       Adenylosuccinate synthetase.
FT                                /FTId=PRO_1000089295.
FT   NP_BIND      12     18       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND      40     42       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND     330    332       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND     412    414       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   REGION       13     16       IMP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   REGION       38     41       IMP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   REGION      298    304       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     13     13       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     41     41       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   METAL        13     13       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   METAL        40     40       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     128    128       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     142    142       IMP; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     223    223       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     238    238       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     302    302       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     304    304       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
SQ   SEQUENCE   427 AA;  45882 MW;  D97FE582CB37C7D4 CRC64;
     MPALVLIGAQ WGDEGKGKAT DLLGGAVDYV VRYQGGNNAG HTVVIGAESY ALHLIPSGVL
     RTDCVPVIGN GVVIDPGVLL SEMDGLQARG VDVSRLLISA DAHLIMPHHR ALDRVTERYL
     GKARIGTTGR GIGPAYGDKV ARTGIRVQDL LDPGIFRQKL ELALREKNQV LTKVYNRRRI
     EVDEVVEEYA AYAERLTPHI ADTGLLLDTA LREGKVVLLE GSQGTLLDVD HGTYPFVTSS
     NPTAGYAATG AGIGPTRINR VIGIIKAYTT RVGAGPFPTE LDDKVGEELR RIGGEFGVTT
     GRARRTGWFD AVIARYAVRV NGLTDLFLTK LDVLSGFDTV PVCVGYEING QRTDEMPMTQ
     TEFHHAKPIY VELPGWHEDI SGVTRFADLP EAAQAYVATL EEMAGAPVSA VGVGPGRAQT
     LVINELI
//

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