(data stored in ACNUC10821 zone)

SWISSPROT: PURA_LISMF

ID   PURA_LISMF              Reviewed;         430 AA.
AC   Q725A8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=LMOf2365_0065;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT02853.1; -; Genomic_DNA.
DR   RefSeq; WP_003724884.1; NC_002973.6.
DR   SMR; Q725A8; -.
DR   EnsemblBacteria; AAT02853; AAT02853; LMOf2365_0065.
DR   KEGG; lmf:LMOf2365_0065; -.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; SNAGHTV; -.
DR   BioCyc; LMON265669:G1G0V-64-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; Q725A8.
DR   SWISS-2DPAGE; Q725A8.
KW   Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    430       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000095195.
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   430 AA;  47619 MW;  CBB523C65F752961 CRC64;
     MSSVVVVGTQ WGDEGKGKIT DFLSENAEAI ARYQGGNNAG HTIKFDGVTY KLHLIPSGIF
     YKEKISVIGN GMVVDPKALV EELKYLHDKG VDTSNLRISN RAHIILPYHI RIDEADEERK
     GANKIGTTKK GIGPAYMDKA ARVGIRIIDL LDKETFKEKL EHNLGEKNRL LERFYELEGF
     KLEDILEEYY DYGQQFKEYV CDTSVVLNDA LDDGKRVLFE GAQGVMLDID QGTYPFVTSS
     NPIAGGVTIG SGVGPSKINH VVGVAKAYTT RVGDGPFPTE LFDTIGDTIR EVGHEYGTTT
     GRPRRVGWFD SVVVRHARRV SGLTDLSLTL LDVLTGIETL KICVAYKLDG KTITEFPASL
     KDLARCEPVY EELPGWTEDI TGVTSLDDLP VNCRHYMERI AQLTGVQVSM FSVGPDRAQT
     HVIKSVWRLA
//

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