PURA_ECOLI
ID PURA_ECOLI Reviewed; 432 AA.
AC P0A7D4; P12283; Q2M6C8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011};
DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011};
DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011};
DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011};
GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; Synonyms=adeK;
GN OrderedLocusNames=b4177, JW4135;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=3058695; DOI=10.1016/s0021-9258(18)37402-7;
RA Wolfe S.A., Smith J.M.;
RT "Nucleotide sequence and analysis of the purA gene encoding
RT adenylosuccinate synthetase of Escherichia coli K12.";
RL J. Biol. Chem. 263:19147-19153(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 146-148, AND MUTAGENESIS OF ARG-148.
RX PubMed=2061308; DOI=10.1016/s0021-9258(18)98886-1;
RA Dong Q., Liu F., Myers A.M., Fromm H.J.;
RT "Evidence for an arginine residue at the substrate binding site of
RT Escherichia coli adenylosuccinate synthetase as studied by chemical
RT modification and site-directed mutagenesis.";
RL J. Biol. Chem. 266:12228-12233(1991).
RN [6]
RP PROTEIN SEQUENCE OF 2-10.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP ACTIVE SITE LYS-141.
RX PubMed=2108156; DOI=10.1016/s0021-9258(19)39315-9;
RA Dong Q., Fromm H.J.;
RT "Chemical modification of adenylosuccinate synthetase from Escherichia coli
RT by pyridoxal 5'-phosphate. Identification of an active site lysyl
RT residue.";
RL J. Biol. Chem. 265:6235-6240(1990).
RN [8]
RP MUTAGENESIS.
RX PubMed=1733940; DOI=10.1016/s0021-9258(18)45891-7;
RA Liu F., Dong Q., Fromm H.J.;
RT "Site-directed mutagenesis of the phosphate-binding consensus sequence in
RT Escherichia coli adenylosuccinate synthetase.";
RL J. Biol. Chem. 267:2388-2392(1992).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SEQUENCE REVISION TO 417.
RX PubMed=7490761; DOI=10.1006/jmbi.1995.0629;
RA Silva M.M., Poland B.W., Hoffman C.R., Fromm H.J., Honzatko R.B.;
RT "Refined crystal structures of unligated adenylosuccinate synthetase from
RT Escherichia coli.";
RL J. Mol. Biol. 254:431-446(1995).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GDP; MAGNESIUM;
RP SUBSTRATE ANALOG AND INHIBITOR.
RX PubMed=8961938; DOI=10.1021/bi961758r;
RA Poland B.W., Lee S.F., Subramanian M.V., Siehl D.L., Anderson R.J.,
RA Fromm H.J., Honzatko R.B.;
RT "Refined crystal structure of adenylosuccinate synthetase from Escherichia
RT coli complexed with hydantocidin 5'-phosphate, GDP, HPO4(2-), Mg2+, and
RT hadacidin.";
RL Biochemistry 35:15753-15759(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-431.
RX PubMed=8663109; DOI=10.1074/jbc.271.26.15407;
RA Poland B.W., Hou Z., Bruns C., Fromm H.J., Honzatko R.B.;
RT "Refined crystal structures of guanine nucleotide complexes of
RT adenylosuccinate synthetase from Escherichia coli.";
RL J. Biol. Chem. 271:15407-15413(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP; IMP; MAGNESIUM
RP AND SUBSTRATE ANALOG.
RX PubMed=9000627; DOI=10.1006/jmbi.1996.0693;
RA Poland B.W., Fromm H.J., Honzatko R.B.;
RT "Crystal structures of adenylosuccinate synthetase from Escherichia coli
RT complexed with GDP, IMP hadacidin, NO3-, and Mg2+.";
RL J. Mol. Biol. 264:1013-1027(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-431.
RX PubMed=8790347; DOI=10.1073/pnas.93.18.9431;
RA Fonne-Pfister R., Chemla P., Ward E., Girardet M., Kreuz K.E.,
RA Honzatko R.B., Fromm H.J., Schaer H.-P., Gruetter M.G., Cowan-Jacob S.W.;
RT "The mode of action and the structure of a herbicide in complex with its
RT target: binding of activated hydantocidin to the feedback regulation site
RT of adenylosuccinate synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9431-9436(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-431.
RX PubMed=9182542; DOI=10.1074/jbc.272.24.15200;
RA Poland B.W., Bruns C., Fromm H.J., Honzatko R.B.;
RT "Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline
RT adenylosuccinate synthetase from Escherichia coli.";
RL J. Biol. Chem. 272:15200-15205(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RX PubMed=10556888;
RX DOI=10.1002/(sici)1521-3773(19991102)38:21<3159::aid-anie3159>3.0.co;2-2;
RA Hanessian S., Lu P.P., Sanceau J.Y., Chemla P., Gohda K., Fonne-Pfister R.,
RA Prade L., Cowan-Jacob S.W.;
RT "An enzyme-bound bisubstrate hybrid inhibitor of adenylosuccinate
RT synthetase.";
RL Angew. Chem. Int. Ed. Engl. 38:3159-3162(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-17;
RP LEU-144 AND LEU-304 IN COMPLEX WITH GTP; IMP; MAGNESIUM AND SUBSTRATE
RP ANALOG.
RX PubMed=10346917; DOI=10.1021/bi990159s;
RA Choe J.Y., Poland B.W., Fromm H.J., Honzatko R.B.;
RT "Mechanistic implications from crystalline complexes of wild-type and
RT mutant adenylosuccinate synthetases from Escherichia coli.";
RL Biochemistry 38:6953-6961(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10364182; DOI=10.1074/jbc.274.25.17505;
RA Hou Z., Cashel M., Fromm H.J., Honzatko R.B.;
RT "Effectors of the stringent response target the active site of Escherichia
RT coli adenylosuccinate synthetase.";
RL J. Biol. Chem. 274:17505-17510(1999).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-432.
RX PubMed=11741996; DOI=10.1074/jbc.m109561200;
RA Hou Z., Wang W., Fromm H.J., Honzatko R.B.;
RT "IMP alone organizes the active site of adenylosuccinate synthetase from
RT Escherichia coli.";
RL J. Biol. Chem. 277:5970-5976(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-431.
RX PubMed=16981730; DOI=10.1021/bi0607498;
RA Iancu C.V., Zhou Y., Borza T., Fromm H.J., Honzatko R.B.;
RT "Cavitation as a mechanism of substrate discrimination by adenylosuccinate
RT synthetases.";
RL Biochemistry 45:11703-11711(2006).
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. {ECO:0000255|HAMAP-Rule:MF_00011}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00011};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011,
CC ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:8961938,
CC ECO:0000269|PubMed:9000627}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00011}.
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DR EMBL; J04199; AAA24446.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97073.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77134.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78178.1; -; Genomic_DNA.
DR PIR; S56402; AJECDS.
DR RefSeq; NP_418598.1; NC_000913.3.
DR RefSeq; WP_000527955.1; NZ_STEB01000013.1.
DR PDB; 1ADE; X-ray; 2.00 A; A/B=2-432.
DR PDB; 1ADI; X-ray; 2.50 A; A/B=2-432.
DR PDB; 1CG0; X-ray; 2.50 A; A=2-432.
DR PDB; 1CG1; X-ray; 2.50 A; A=2-432.
DR PDB; 1CG3; X-ray; 2.50 A; A=2-432.
DR PDB; 1CG4; X-ray; 2.50 A; A=2-432.
DR PDB; 1CH8; X-ray; 2.50 A; A=2-432.
DR PDB; 1CIB; X-ray; 2.30 A; A=2-432.
DR PDB; 1GIM; X-ray; 2.50 A; A=2-432.
DR PDB; 1GIN; X-ray; 2.80 A; A=2-432.
DR PDB; 1HON; X-ray; 2.30 A; A/B=2-432.
DR PDB; 1HOO; X-ray; 2.30 A; A/B=2-432.
DR PDB; 1HOP; X-ray; 2.30 A; A/B=2-432.
DR PDB; 1JUY; X-ray; 2.50 A; A=2-432.
DR PDB; 1KJX; X-ray; 2.60 A; A=1-432.
DR PDB; 1KKB; X-ray; 2.60 A; A=1-432.
DR PDB; 1KKF; X-ray; 2.60 A; A=1-432.
DR PDB; 1KSZ; X-ray; 2.80 A; A=2-432.
DR PDB; 1NHT; X-ray; 2.50 A; A=2-432.
DR PDB; 1QF4; X-ray; 2.20 A; A=2-432.
DR PDB; 1QF5; X-ray; 2.00 A; A=2-432.
DR PDB; 1SON; X-ray; 2.55 A; A=2-432.
DR PDB; 1SOO; X-ray; 2.60 A; A=2-432.
DR PDB; 2GCQ; X-ray; 2.00 A; A=2-432.
DR PDBsum; 1ADE; -.
DR PDBsum; 1ADI; -.
DR PDBsum; 1CG0; -.
DR PDBsum; 1CG1; -.
DR PDBsum; 1CG3; -.
DR PDBsum; 1CG4; -.
DR PDBsum; 1CH8; -.
DR PDBsum; 1CIB; -.
DR PDBsum; 1GIM; -.
DR PDBsum; 1GIN; -.
DR PDBsum; 1HON; -.
DR PDBsum; 1HOO; -.
DR PDBsum; 1HOP; -.
DR PDBsum; 1JUY; -.
DR PDBsum; 1KJX; -.
DR PDBsum; 1KKB; -.
DR PDBsum; 1KKF; -.
DR PDBsum; 1KSZ; -.
DR PDBsum; 1NHT; -.
DR PDBsum; 1QF4; -.
DR PDBsum; 1QF5; -.
DR PDBsum; 1SON; -.
DR PDBsum; 1SOO; -.
DR PDBsum; 2GCQ; -.
DR AlphaFoldDB; P0A7D4; -.
DR SMR; P0A7D4; -.
DR BioGRID; 4262696; 52.
DR BioGRID; 852987; 1.
DR DIP; DIP-36219N; -.
DR IntAct; P0A7D4; 3.
DR STRING; 511145.b4177; -.
DR DrugBank; DB02666; (C8-R)-hydantocidin 5'-phosphate.
DR DrugBank; DB04460; (C8-S)-Hydantocidin 5'-phosphate.
DR DrugBank; DB02954; (Carboxyhydroxyamino)Ethanoic Acid.
DR DrugBank; DB03146; 2-deazo-6-thiophosphate guanosine-5'-monophosphate.
DR DrugBank; DB02836; Guanosine 5'-diphosphate 2':3'-cyclic monophosphate.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB02109; Hadacidin.
DR DrugBank; DB02493; Hydantocidin-5'-phosphate.
DR DrugBank; DB04566; Inosinic Acid.
DR CarbonylDB; P0A7D4; -.
DR SWISS-2DPAGE; P0A7D4; -.
DR jPOST; P0A7D4; -.
DR PaxDb; P0A7D4; -.
DR PRIDE; P0A7D4; -.
DR EnsemblBacteria; AAC77134; AAC77134; b4177.
DR EnsemblBacteria; BAE78178; BAE78178; BAE78178.
DR GeneID; 66671910; -.
DR GeneID; 948695; -.
DR KEGG; ecj:JW4135; -.
DR KEGG; eco:b4177; -.
DR PATRIC; fig|1411691.4.peg.2524; -.
DR EchoBASE; EB0783; -.
DR eggNOG; COG0104; Bacteria.
DR HOGENOM; CLU_029848_0_0_6; -.
DR InParanoid; P0A7D4; -.
DR OMA; FHHAKPI; -.
DR PhylomeDB; P0A7D4; -.
DR BioCyc; EcoCyc:ADENYLOSUCCINATE-SYN-MON; -.
DR BioCyc; MetaCyc:ADENYLOSUCCINATE-SYN-MON; -.
DR BRENDA; 6.3.4.4; 2026.
DR SABIO-RK; P0A7D4; -.
DR UniPathway; UPA00075; UER00335.
DR EvolutionaryTrace; P0A7D4; -.
DR PRO; PR:P0A7D4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0046086; P:adenosine biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoliWiki.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:EcoCyc.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR Gene3D; 3.90.170.10; -; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00184; purA; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3058695,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..432
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000095174"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT ACT_SITE 42
FT /note="Proton donor"
FT BINDING 13..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917"
FT BINDING 14..17
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:8961938,
FT ECO:0000269|PubMed:9000627"
FT BINDING 39..42
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 41..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:8961938,
FT ECO:0000269|PubMed:9000627"
FT BINDING 130
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627"
FT BINDING 144
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627"
FT BINDING 225
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627"
FT BINDING 240
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627"
FT BINDING 300..306
FT /ligand="substrate"
FT BINDING 304
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917, ECO:0000269|PubMed:9000627"
FT BINDING 306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917"
FT BINDING 332..334
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917"
FT BINDING 415..417
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011,
FT ECO:0000269|PubMed:10346917"
FT MUTAGEN 13
FT /note="G->V: Significant reduction in activity."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 16
FT /note="G->V: Significant reduction in activity."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 17
FT /note="K->Q: Reduces catalytic efficiency by 50%."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 18
FT /note="G->V: Significant reduction in activity."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 19
FT /note="K->R: Significant reduction in activity."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 20
FT /note="I->T: Significant reduction in activity."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 141
FT /note="K->I: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 144
FT /note="R->L: Does not reduce catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:1733940"
FT MUTAGEN 148
FT /note="R->L: Reduced activity."
FT /evidence="ECO:0000269|PubMed:2061308"
FT MUTAGEN 304
FT /note="R->L: Reduces catalytic efficiency by 87%."
FT /evidence="ECO:0000269|PubMed:1733940"
FT CONFLICT 417
FT /note="G -> D (in Ref. 1; AAA24446)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1ADE"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1HOO"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1GIM"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1HOP"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1QF5"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 155..175
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1ADE"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1ADI"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:1ADE"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1QF5"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:1ADE"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:1ADE"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:1ADE"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:1ADE"
SQ SEQUENCE 432 AA; 47345 MW; AAA862CA0F80DA70 CRC64;
MGNNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI
LRENVTSIIG NGVVLSPAAL MKEMKELEDR GIPVRERLLL SEACPLILDY HVALDNAREK
ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFDKETFAE KLKEVMEYHN FQLVNYYKAE
AVDYQKVLDD TMAVADILTS MVVDVSDLLD QARQRGDFVM FEGAQGTLLD IDHGTYPYVT
SSNTTAGGVA TGSGLGPRYV DYVLGILKAY STRVGAGPFP TELFDETGEF LCKQGNEFGA
TTGRRRRTGW LDTVAVRRAV QLNSLSGFCL TKLDVLDGLK EVKLCVAYRM PDGREVTTTP
LAADDWKGVE PIYETMPGWS ESTFGVKDRS GLPQAALNYI KRIEELTGVP IDIISTGPDR
TETMILRDPF DA
