(data stored in ACNUC7421 zone)

SWISSPROT: E3J4W9_FRAIE

ID   E3J4W9_FRAIE            Unreviewed;       427 AA.
AC   E3J4W9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE            Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_00011};
DE            Short=AdSS {ECO:0000256|HAMAP-Rule:MF_00011};
DE            EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE   AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011};
GN   Name=purA {ECO:0000256|HAMAP-Rule:MF_00011};
GN   OrderedLocusNames=FraEuI1c_0200 {ECO:0000313|EMBL:ADP78288.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78288.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78288.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00011};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011,
CC       ECO:0000256|RuleBase:RU000520}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}.
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DR   EMBL; CP002299; ADP78288.1; -; Genomic_DNA.
DR   RefSeq; WP_013421411.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0200; -.
DR   EnsemblBacteria; ADP78288; ADP78288; FraEuI1c_0200.
DR   KEGG; fri:FraEuI1c_0200; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; SNAGHTV; -.
DR   OrthoDB; 232152at2; -.
DR   BioCyc; FSP298654:G1GOT-203-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000002484; 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; E3J4W9.
DR   SWISS-2DPAGE; E3J4W9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520, ECO:0000313|EMBL:ADP78288.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   NP_BIND      12     18       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND      40     42       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     330    332       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     412    414       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   REGION       13     16       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION       38     41       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION      298    304       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     13     13       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE     41     41       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE    139    139       {ECO:0000256|PROSITE-ProRule:PRU10134}.
FT   METAL        13     13       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   METAL        40     40       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     128    128       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     142    142       IMP; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     223    223       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     238    238       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     302    302       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     304    304       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
SQ   SEQUENCE   427 AA;  45719 MW;  204AF06E08CFB888 CRC64;
     MPALVLIGAQ WGDEGKGKAT DLLGGAVDYV VRYQGGNNAG HTVVIGAEKY ALHLIPSGIL
     RPDCVPVIGN GVVIDPGVLL AEMAGLRARG IDTSRLLISA SAHLIMPHHR ALDRVTERYL
     GKARIGTTGR GIGPAYGDKV ARTGIRVQDL LDPGILRQKL ELALREKNQV LAKVYNRRKI
     EVDAVVAEYL DYASQLGPHI ADTGLVLDTA LRAGKVVLLE GSQGTLLDVD HGTYPFVTSS
     NPTAGGAATG AGIGPTRISR VIGIIKAYTT RVGSGPFPTE LDDKVGDELR RIGGEFGVTT
     GRARRTGWYD AVIARYAVRV NGLTDLFLTK LDVLSGFDTV PVCVAYDVGG TRMAEMPMTQ
     TEFHHAKPIY EEFPGWHEDI SEATSFDQLP PEARDYVRAL EEMSGAPISA IGVGPGRDQT
     LVLRDLL
//

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