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Adenylosuccinate synthetase (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase)

 J7YA76_BACCE            Unreviewed;       429 AA.
J7YA76;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
28-MAR-2018, entry version 36.
RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_00011};
Short=AdSS {ECO:0000256|HAMAP-Rule:MF_00011};
EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011};
Name=purA {ECO:0000256|HAMAP-Rule:MF_00011};
ORFNames=IEE_00028 {ECO:0000313|EMBL:EJQ53808.1};
Bacillus cereus BAG5X1-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ53808.1, ECO:0000313|Proteomes:UP000006600};
[1] {ECO:0000313|EMBL:EJQ53808.1, ECO:0000313|Proteomes:UP000006600}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ53808.1,
ECO:0000313|Proteomes:UP000006600};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V.,
Timmery S., Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X.,
Shank E.B., Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q.,
Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Bacillus cereus BAG5X1-1.";
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays an important role in the de novo pathway of purine
nucleotide biosynthesis. Catalyzes the first committed step in the
biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
-!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00011};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00011};
-!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00011}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}.
-!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
{ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJQ53808.1}.
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EMBL; AHDJ01000001; EJQ53808.1; -; Genomic_DNA.
RefSeq; WP_002113221.1; NZ_JH791996.1.
EnsemblBacteria; EJQ53808; EJQ53808; IEE_00028.
PATRIC; fig|1053189.3.peg.28; -.
UniPathway; UPA00075; UER00335.
Proteomes; UP000006600; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd03108; AdSS; 1.
HAMAP; MF_00011; Adenylosucc_synth; 1.
InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
InterPro; IPR001114; Adenylosuccinate_synthetase.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11846; PTHR11846; 1.
Pfam; PF00709; Adenylsucc_synt; 1.
SMART; SM00788; Adenylsucc_synt; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00184; purA; 1.
PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006600};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520};
Ligase {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00011,
ECO:0000256|RuleBase:RU000520}.
NP_BIND 12 18 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
NP_BIND 40 42 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
NP_BIND 330 332 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
NP_BIND 412 414 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
REGION 13 16 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_00011}.
REGION 38 41 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_00011}.
REGION 298 304 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00011}.
COILED 157 177 {ECO:0000256|SAM:Coils}.
ACT_SITE 13 13 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00011}.
ACT_SITE 41 41 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00011}.
ACT_SITE 139 139 {ECO:0000256|PROSITE-ProRule:PRU10134}.
METAL 13 13 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00011}.
METAL 40 40 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 128 128 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 142 142 IMP; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 223 223 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 238 238 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 302 302 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 304 304 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
SEQUENCE 429 AA; 47541 MW; 3CE5B715A4D44012 CRC64;
MSSVVVVGTQ WGDEGKGKIT DFLSEHAEVV ARYQGGNNAG HTIVFGGVKY KLHLIPSGIF
YKEKICVIGN GLVVDPKALL EELKYLHDRG VSTDNLRVSN RAHVILPYHL KQDELEEASK
GDNKIGTTKK GIGPAYMDKA ARIGIRMADL LDREAFKEKL ERNLVEKNRL FEKMYDTEGF
SVEEIFEEYF EYGQQIAHYV CDTSVVLNDA LDNNHRVLFE GAQGVMLDID HGTYPFVTSS
NPIAGGVTVG TGVGPAKVTR VVGVCKAYTS RVGDGPFPTE LNDEIGHQIR EVGREYGTTT
GRPRRVGWFD SVVVRHARRV SGLTDLSLNS IDVLTGIPTL KICVAYKYNG EVIDEVPANL
NILAKCEPVY EELPGWEEDI TGVKSLDELP ENARKYVERV SELTGIQLSM FSVGPDRNQT
NIVRNVYEA


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