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Database: UniProt/SWISS-PROT
Entry: PURA_BORPE
LinkDB: PURA_BORPE
Original site: PURA_BORPE 
ID   PURA_BORPE              Reviewed;         435 AA.
AC   Q7VWM1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   14-MAY-2014, entry version 67.
DE   RecName: Full=Adenylosuccinate synthetase;
DE            Short=AMPSase;
DE            Short=AdSS;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase;
GN   Name=purA; Synonyms=adeK; OrderedLocusNames=BP2188;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
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DR   EMBL; BX640417; CAE42466.1; -; Genomic_DNA.
DR   RefSeq; NP_880836.1; NC_002929.2.
DR   ProteinModelPortal; Q7VWM1; -.
DR   SMR; Q7VWM1; 6-434.
DR   STRING; 257313.BP2188; -.
DR   EnsemblBacteria; CAE42466; CAE42466; BP2188.
DR   GeneID; 2666913; -.
DR   KEGG; bpe:BP2188; -.
DR   PATRIC; 21157750; VBIBorPer7866_2362.
DR   eggNOG; COG0104; -.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; IERCTPV; -.
DR   OrthoDB; EOG68Q0QG; -.
DR   BioCyc; BPER257313:BP2188-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR018220; Adenylosuccinate_synthase_AS.
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;
KW   Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    435       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000095151.
FT   NP_BIND      17     23       GTP (By similarity).
FT   NP_BIND      45     47       GTP (By similarity).
FT   NP_BIND     336    338       GTP (By similarity).
FT   NP_BIND     418    420       GTP (By similarity).
FT   REGION       18     21       IMP binding (By similarity).
FT   REGION       43     46       IMP binding (By similarity).
FT   REGION      304    310       Substrate binding (By similarity).
FT   ACT_SITE     18     18       Proton acceptor (By similarity).
FT   ACT_SITE     46     46       Proton donor (By similarity).
FT   METAL        18     18       Magnesium (By similarity).
FT   METAL        45     45       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     134    134       IMP (By similarity).
FT   BINDING     148    148       IMP; shared with dimeric partner (By
FT                                similarity).
FT   BINDING     229    229       IMP (By similarity).
FT   BINDING     244    244       IMP (By similarity).
FT   BINDING     308    308       IMP (By similarity).
FT   BINDING     310    310       GTP (By similarity).
SQ   SEQUENCE   435 AA;  46776 MW;  F35A4158E82013C2 CRC64;
     MIRKMSKNVV VIGTQWGDEG KGKIVDWLAE SVQGVVRFQG GHNAGHTLWI NGKKTILRLI
     PSGIMHDGVT CFIGNGVVLS PEALLREIEE LEAAGLDVRS RLQVSEICTL ILPYHVAVDK
     AREARKGEGK IGTTGRGIGP AYEDKVARRA LRVQDLFNPA LFDEKLAEVL DYHNFVLTQY
     LGAEPVSANE VRDQAMALAP ALAPMVRDVS SNLFALQQEG KNLLFEGAQG ALLDVDHGTY
     PFVTSSNCVA GAASAGAGVG PQALQYVLGI TKAYTTRVGS GPFPTELVDE IGARLATIGK
     EFGSVTGRPR RCGWLDGAAL KRSVRLNGIS GLCITKLDVL DGLETIQLGV GYRVNGEFRD
     VLPYGAHAVA QAQAVLEELP GWTESTVGIT EYSKLPVNAR RYLERVAEVC GVPIDLVSTG
     PDRNKTIVLR HPFKG
//
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