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

 A0A084G0Z5_9PEZI        Unreviewed;       428 AA.
A0A084G0Z5;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
27-SEP-2017, entry version 20.
RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_03125};
Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_03125};
Short=AdSS {ECO:0000256|HAMAP-Rule:MF_03125};
EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03125};
AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_03125};
ORFNames=SAPIO_CDS7035 {ECO:0000313|EMBL:KEZ41007.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ41007.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ41007.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ41007.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays an important role in the de novo pathway and in
the salvage pathway of purine nucleotide biosynthesis. Catalyzes
the first commited step in the biosynthesis of AMP from IMP.
{ECO:0000256|HAMAP-Rule:MF_03125}.
-!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03125};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_03125};
-!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03125}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03125}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125}.
-!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
{ECO:0000256|HAMAP-Rule:MF_03125}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ41007.1}.
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EMBL; JOWA01000110; KEZ41007.1; -; Genomic_DNA.
RefSeq; XP_016640806.1; XM_016788979.1.
EnsemblFungi; KEZ41007; KEZ41007; SAPIO_CDS7035.
GeneID; 27726107; -.
UniPathway; UPA00075; UER00335.
Proteomes; UP000028545; 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; 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.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_03125};
Ligase {ECO:0000256|HAMAP-Rule:MF_03125};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03125};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03125};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03125};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03125};
Reference proteome {ECO:0000313|Proteomes:UP000028545}.
NP_BIND 13 19 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
NP_BIND 41 43 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
NP_BIND 330 332 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
NP_BIND 414 416 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
REGION 14 17 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03125}.
REGION 39 42 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03125}.
REGION 298 304 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03125}.
ACT_SITE 14 14 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03125}.
ACT_SITE 42 42 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_03125}.
METAL 14 14 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_03125}.
METAL 41 41 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03125}.
BINDING 131 131 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
BINDING 145 145 IMP; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_03125}.
BINDING 223 223 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
BINDING 238 238 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
BINDING 302 302 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
BINDING 304 304 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
SEQUENCE 428 AA; 46975 MW; 2AEA023A4591B95F CRC64;
MGSIDVVLGA AWGDEGKGKL VDILSGTAQI CARAQGGHNA GHSIVANGVS YDFHLLPSGL
MNPNCLNLIG SGVVVHVPTF FSELETVEKK GLQNVHSRIF ISDRCHIDFD LHCAVDAAEE
LELGSESIGT TKRGIGPCYA SMATRSGITM SEMFRPDVFE HRLRKLADAY KKRFGDKLVY
DVEDEIERFK GYRERLANYV IDAVTFMNDA QQRGARILIE GSQAIMLDVN YGTYPYVTSS
NTGLGGIIVG LGLNPRKLGD VIGTVKAYTT RVGAGPFATE DTGAVGTHLQ EVGREWGVST
GRRRRCGWLD LVQIKYSHML NHYTALNLTK LDVLDDMETI KVAVGYKNPQ TGAELPTFPA
DMDLLGQVEV VYKELPGWKA STSKVQKFEE LPKGAQDYIK FIEEYVGVRI RWIGTGPGRE
DMIDRGSS


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