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

 PURA_YEAST              Reviewed;         433 AA.
P80210; D6W0X0;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 161.
RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03125};
Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_03125};
Short=AS-synthetase;
Short=AdSS {ECO:0000255|HAMAP-Rule:MF_03125};
EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03125};
AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_03125};
Name=ADE12 {ECO:0000255|HAMAP-Rule:MF_03125};
OrderedLocusNames=YNL220W; ORFNames=N1290;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7603488;
Andreichuk I.V., Shabes A.V., Ryzhova T.A., Kotova I.A., Domkin V.D.;
"Saccharomyces cerevisiae ADE12 gene, coding for adenylosuccinate
synthetase (EC 6.3.4.4). Cloning, sequencing, expression, and
superproduction.";
Mol. Genet. Mikrobiol. Virusol. 1:21-28(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INHIBITION BY SS-DNA, AND SUBUNIT.
PubMed=8706758; DOI=10.1111/j.1432-1033.1996.0487u.x;
Gallert K.C., Ohanjan T., Daignan-Fornier B., Lottspeich F.,
Krauss G.;
"Enzymatic properties and inhibition by single-stranded autonomously
replicating sequences of adenylosuccinate synthase from Saccharomyces
cerevisiae.";
Eur. J. Biochem. 239:487-493(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 2-23 AND 234-245.
PubMed=8376380;
Zeidler R., Hobert O., Johannes L., Faulhammer H., Krauss G.;
"Characterization of two novel single-stranded DNA-specific
autonomously replicating sequence-binding proteins from Saccharomyces
cerevisiae, one of which is adenylosuccinate synthetase.";
J. Biol. Chem. 268:20191-20197(1993).
[6]
PROTEIN SEQUENCE OF 2-6, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, AND ENZYME REGULATION.
PubMed=10417315; DOI=10.1042/bj3410537;
Lipps G., Krauss G.;
"Adenylosuccinate synthase from Saccharomyces cerevisiae: homologous
overexpression, purification and characterization of the recombinant
protein.";
Biochem. J. 341:537-543(1999).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=9668204;
Ryzhova T.A., Andreichuk Y.V., Domkin V.D.;
"Adenylosuccinate synthetase of the yeast Saccharomyces cerevisiae:
purification and properties.";
Biochemistry (Mosc.) 63:650-656(1998).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Plays an important role in the de novo pathway and in
the salvage pathway of purine nucleotide biosynthesis. Catalyzes
the first committed step in the biosynthesis of AMP from IMP.
{ECO:0000269|PubMed:10417315, ECO:0000269|PubMed:9668204}.
-!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-Rule:MF_03125}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03125};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_03125};
-!- ENZYME REGULATION: Inhibited by GMP. Inhibited by chloride.
Inhibited in a highly specific manner by the binding of a 44-base
DNA oligonucleotide carrying the ARS core consensus sequence.
{ECO:0000269|PubMed:10417315}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1650 uM for L-aspartate {ECO:0000269|PubMed:10417315,
ECO:0000269|PubMed:9668204};
KM=200 uM for IMP {ECO:0000269|PubMed:10417315,
ECO:0000269|PubMed:9668204};
KM=1650 uM for GTP {ECO:0000269|PubMed:10417315,
ECO:0000269|PubMed:9668204};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:10417315,
ECO:0000269|PubMed:9668204};
Temperature dependence:
Optimum temperature is 35 degrees Celsius.
{ECO:0000269|PubMed:10417315, ECO:0000269|PubMed:9668204};
-!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03125}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03125,
ECO:0000269|PubMed:10417315, ECO:0000269|PubMed:8706758,
ECO:0000269|PubMed:9668204}.
-!- INTERACTION:
P33203:PRP40; NbExp=2; IntAct=EBI-14267, EBI-701;
P39940:RSP5; NbExp=2; IntAct=EBI-14267, EBI-16219;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03125,
ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 56800 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
{ECO:0000255|HAMAP-Rule:MF_03125}.
-----------------------------------------------------------------------
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EMBL; L22185; AAA91338.1; -; Genomic_DNA.
EMBL; Z48671; CAA88590.1; -; Genomic_DNA.
EMBL; Z71496; CAA96123.1; -; Genomic_DNA.
EMBL; BK006947; DAA10336.1; -; Genomic_DNA.
PIR; S48515; S48515.
RefSeq; NP_014179.1; NM_001183058.1.
ProteinModelPortal; P80210; -.
SMR; P80210; -.
BioGrid; 35616; 144.
DIP; DIP-4286N; -.
IntAct; P80210; 8.
MINT; MINT-560386; -.
STRING; 4932.YNL220W; -.
iPTMnet; P80210; -.
MaxQB; P80210; -.
PRIDE; P80210; -.
EnsemblFungi; YNL220W; YNL220W; YNL220W.
GeneID; 855501; -.
KEGG; sce:YNL220W; -.
EuPathDB; FungiDB:YNL220W; -.
SGD; S000005164; ADE12.
GeneTree; ENSGT00390000015553; -.
HOGENOM; HOG000260959; -.
InParanoid; P80210; -.
KO; K01939; -.
OMA; GVSKAYT; -.
OrthoDB; EOG092C2D4T; -.
BioCyc; MetaCyc:YNL220W-MONOMER; -.
BioCyc; YEAST:YNL220W-MONOMER; -.
Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis.
UniPathway; UPA00075; UER00335.
PRO; PR:P80210; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:SGD.
GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:SGD.
GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
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.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding;
Ligase; Magnesium; Metal-binding; Nucleotide-binding;
Purine biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10417315,
ECO:0000269|PubMed:8376380}.
CHAIN 2 433 Adenylosuccinate synthetase.
/FTId=PRO_0000095138.
NP_BIND 11 17 GTP. {ECO:0000255|HAMAP-Rule:MF_03125}.
NP_BIND 39 41 GTP. {ECO:0000255|HAMAP-Rule:MF_03125}.
NP_BIND 337 339 GTP. {ECO:0000255|HAMAP-Rule:MF_03125}.
NP_BIND 419 421 GTP. {ECO:0000255|HAMAP-Rule:MF_03125}.
REGION 12 15 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03125}.
REGION 37 40 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03125}.
REGION 305 311 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03125}.
ACT_SITE 12 12 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03125}.
ACT_SITE 40 40 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_03125}.
METAL 12 12 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_03125}.
METAL 39 39 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03125}.
BINDING 134 134 IMP. {ECO:0000255|HAMAP-Rule:MF_03125}.
BINDING 148 148 IMP; shared with dimeric partner.
{ECO:0000255|HAMAP-Rule:MF_03125}.
BINDING 230 230 IMP. {ECO:0000255|HAMAP-Rule:MF_03125}.
BINDING 245 245 IMP. {ECO:0000255|HAMAP-Rule:MF_03125}.
BINDING 309 309 IMP. {ECO:0000255|HAMAP-Rule:MF_03125}.
BINDING 311 311 GTP. {ECO:0000255|HAMAP-Rule:MF_03125}.
CONFLICT 237 237 D -> G (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 433 AA; 48279 MW; 800E0F4062D9856F CRC64;
MVNVVLGSQW GDEGKGKLVD LLVGKYDIVA RCAGGNNAGH TIVVDGVKYD FHMLPSGLVN
PNCQNLLGNG VVIHVPSFFK ELETLEAKGL KNARSRLFVS SRAHLVFDFH QVTDKLRELE
LSGRSKDGKN IGTTGKGIGP TYSTKASRSG LRVHHLVNDQ PGAWEEFVAR YKRLLETRRQ
RYGDFEYDFE AKLAEYKKLR EQLKPFVVDS VVFMHNAIEA KKKILVEGAN ALMLDIDFGT
YPYVTSSNTG IGGVLTGLGI PPRTIDEIYG VVKAYTTRVG EGPFPTEQLN ENGEKLQTIG
AEFGVTTGRK RRCGWLDLVV LKYSTLINGY TSLNITKLDV LDTFKEIPVG ISYSIQGKKL
DLFPEDLNIL GKVEVEYKVL PGWDQDITKI TKYEDLPENA KKYLKYIEDF VGVPVEWVGT
GPARESMLHK EIK


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