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 01-MAY-2013, entry version 62.
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; LDYYNFQ; -.
DR ProtClustDB; PRK01117; -.
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:HAMAP.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA: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 PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 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
//
