(data stored in SCRATCH3701 zone)

SWISSPROT: PURA_LISMO

ID   PURA_LISMO              Reviewed;         430 AA.
AC   Q8YAR1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 108.
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=lmo0055;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591973; CAC98270.1; -; Genomic_DNA.
DR   PIR; AH1081; AH1081.
DR   RefSeq; NP_463588.1; NC_003210.1.
DR   RefSeq; WP_003721679.1; NC_003210.1.
DR   SMR; Q8YAR1; -.
DR   STRING; 169963.lmo0055; -.
DR   PaxDb; Q8YAR1; -.
DR   EnsemblBacteria; CAC98270; CAC98270; CAC98270.
DR   GeneID; 986069; -.
DR   KEGG; lmo:lmo0055; -.
DR   PATRIC; fig|169963.11.peg.57; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; FHHAKPI; -.
DR   PhylomeDB; Q8YAR1; -.
DR   BioCyc; LMON169963:LMO0055-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
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; Q8YAR1.
DR   SWISS-2DPAGE; Q8YAR1.
KW   Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..430
FT                   /note="Adenylosuccinate synthetase"
FT                   /id="PRO_0000095196"
FT   NP_BIND         12..18
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         40..42
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         330..332
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         412..414
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          13..16
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          38..41
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          298..304
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   ACT_SITE        13
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   ACT_SITE        41
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   METAL           13
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   METAL           40
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         128
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         142
FT                   /note="IMP; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         223
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         238
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         302
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         304
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
SQ   SEQUENCE   430 AA;  47605 MW;  4BD92771D104BE7D CRC64;
     MSSVVVVGTQ WGDEGKGKIT DFLSENAEAI ARYQGGNNAG HTIKFDGVTY KLHLIPSGIF
     YKEKISVIGN GMVVDPKALV EELKYLHDKG VDTSNLRISN RAHIILPYHI RIDEADEERK
     GANKIGTTKK GIGPAYMDKA ARVGIRIIDL LDKETFKEKL EHNLGEKNRL LERFYELEGF
     KLEDILDEYY EYGQQFKEYV CDTSVVLNDA LDDGKRVLFE GAQGVMLDID QGTYPFVTSS
     NPIAGGVTIG SGVGPSKINH VVGVAKAYTT RVGDGPFPTE LFDSIGDTIR EVGHEYGTTT
     GRPRRVGWFD SVVVRHARRV SGLTDLSLTL LDVLTGIETL KICVAYKLDG KTITEFPASL
     KDLARCEPVY EELPGWTEDI TGVTSLDDLP VNCRHYMERI AQLTGVQVSM FSVGPDRAQT
     HVIKSVWRLA
//

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