(data stored in ACNUC7421 zone)

SWISSPROT: PURA_LEGPC

ID   PURA_LEGPC              Reviewed;         431 AA.
AC   A5IHA9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 78.
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=LPC_2858;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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}.
DR   EMBL; CP000675; ABQ56759.1; -; Genomic_DNA.
DR   RefSeq; WP_011945645.1; NC_009494.2.
DR   SMR; A5IHA9; -.
DR   PRIDE; A5IHA9; -.
DR   EnsemblBacteria; ABQ56759; ABQ56759; LPC_2858.
DR   KEGG; lpc:LPC_2858; -.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; FHHAKPI; -.
DR   BioCyc; LPNE400673:LPC_RS02675-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
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; A5IHA9.
DR   SWISS-2DPAGE; A5IHA9.
KW   Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..431
FT                   /note="Adenylosuccinate synthetase"
FT                   /id="PRO_1000000849"
FT   NP_BIND         13..19
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         41..43
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         332..334
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         415..417
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          14..17
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          39..42
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          300..306
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   ACT_SITE        42
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   METAL           14
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   METAL           41
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         130
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         144
FT                   /note="IMP; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         225
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         240
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         304
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         306
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
SQ   SEQUENCE   431 AA;  47467 MW;  9EB3C0A20B2525F5 CRC64;
     MGKNVVVLGT QWGDEGKGKI VDLLTQDAQV VVRYQGGHNA GHTLKINGVK TVLRLIPSGM
     LRPNVTCYIA NGVVLSPQAL LSEIKELEGN GVNVRERLRI SLACPLILPY HIALDKARET
     HMGKSAIGTT GRGIGPAYED KVARRALRVG DLFHRDRFAN KLTELLDYHN FVLTQYFKQP
     AVDLESLLDE SLQWVEELRP MVCDVSACLH EHRKQGENIL FEGAQGVYLD IDHGTYPYVT
     SSNTCVGSVI NGAGFGPRYI DYVLGITKAY TTRVGGGPFP TELLDDVGKR IAERGQEFGA
     VTGRPRRCGW FDAVLLKRSI ELNSISGLCV TKLDVLDGLE VLRIAVAYKD RDGNILSRPP
     LAADDFNDLL PVYEELPGWQ ESTADVTLMS DLPANARAYL KRIEEILGIP IDMLSTGPER
     DSTITLRGPF L
//

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