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

 H0BFW5_9ACTN            Unreviewed;       423 AA.
H0BFW5;
22-FEB-2012, integrated into UniProtKB/TrEMBL.
22-FEB-2012, sequence version 1.
28-MAR-2018, entry version 37.
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=SPW_4152 {ECO:0000313|EMBL:EHM27429.1};
Streptomyces sp. W007.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1055352 {ECO:0000313|EMBL:EHM27429.1, ECO:0000313|Proteomes:UP000004626};
[1] {ECO:0000313|EMBL:EHM27429.1, ECO:0000313|Proteomes:UP000004626}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=W007 {ECO:0000313|EMBL:EHM27429.1,
ECO:0000313|Proteomes:UP000004626};
PubMed=22374958; DOI=10.1128/JB.06701-11;
Qin S., Zhang H., Li F., Zhu B., Zheng H.;
"Draft Genome Sequence of Marine Streptomyces sp. Strain W007, Which
Produces Angucyclinone Antibiotics with a Benz[a]anthracene
Skeleton.";
J. Bacteriol. 194:1628-1629(2012).
-!- 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:EHM27429.1}.
-----------------------------------------------------------------------
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EMBL; AGSW01000147; EHM27429.1; -; Genomic_DNA.
EnsemblBacteria; EHM27429; EHM27429; SPW_4152.
PATRIC; fig|1055352.3.peg.4247; -.
UniPathway; UPA00075; UER00335.
Proteomes; UP000004626; 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:UP000004626};
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 8 14 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
NP_BIND 36 38 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
NP_BIND 326 328 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
NP_BIND 408 410 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
REGION 9 12 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_00011}.
REGION 34 37 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_00011}.
REGION 294 300 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00011}.
COILED 153 173 {ECO:0000256|SAM:Coils}.
ACT_SITE 9 9 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00011}.
ACT_SITE 37 37 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00011}.
ACT_SITE 135 135 {ECO:0000256|PROSITE-ProRule:PRU10134}.
METAL 9 9 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00011}.
METAL 36 36 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 124 124 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 138 138 IMP; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 219 219 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 234 234 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 298 298 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
BINDING 300 300 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
SEQUENCE 423 AA; 45524 MW; E2285F7817FBBD91 CRC64;
MLLGAQWGDE GKGKATDLLG GSVDYVVRYQ GGNNAGHTVV VGDQKYALHL LPSGILSPGC
TPVIGNGVVV DPAVLLSELS GLNERGVDTS KLLISGNAHL ITPYNVTLDK VTERFLGKRK
IGTTGRGIGP TYADKINRVG IRVQDLYDES ILVQKVEAAL EQKNQLLAKV FNRRAIEAGK
VVEDMLQYAE QIKPFVADTT LILNDAIDEG KVVLFEGGQG TLLDVDHGTY PFVTSSNPTA
GGACTGAGVG PTKISRVIGI LKAYTTRVGA GPFPTELHDE DGEALRRIGG ERGVTTGRDR
RCGWFDAPIA RYATRVNGLT DFFLTKLDVL TGWEQIPVCV AYEIDGKRVE ELPYNQTDFH
HAKPIYENLP GWSEDITKAK TFADLPKNAQ AYVKALEEMS GAPISAIGVG PGRTETIEIN
SFL


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