PURA_YERP3
ID PURA_YERP3 Reviewed; 432 AA.
AC A7FMX4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=YpsIP31758_3648;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00011};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00011};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00011}.
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DR EMBL; CP000720; ABS46775.1; -; Genomic_DNA.
DR RefSeq; WP_012105751.1; NC_009708.1.
DR AlphaFoldDB; A7FMX4; -.
DR SMR; A7FMX4; -.
DR EnsemblBacteria; ABS46775; ABS46775; YpsIP31758_3648.
DR KEGG; ypi:YpsIP31758_3648; -.
DR HOGENOM; CLU_029848_0_0_6; -.
DR OMA; FHHAKPI; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000002412; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..432
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_1000057093"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT ACT_SITE 42
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 13..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 41..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
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 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 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 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 BINDING 300..306
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
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 BINDING 306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 332..334
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 415..417
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
SQ SEQUENCE 432 AA; 47292 MW; 94FDDA043366A931 CRC64;
MGKNVVVLGT QWGDEGKGKV VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI
LRENVISIIG NGVVLAPDAL MKEMTELEAR GVPVRERLLL SEACPLILPY HVALDNAREK
ARGAKAIGTT GRGIGPAYED KVARRGLRVS DLFNKETFAI KLKEIVEYHN FQLVHYYKEA
AVDYQKVLDD VLAIADILTA MVVDVSELLD NARKQGELIM FEGAQGTLLD IDHGTYPYVT
SSNTTAGGVA TGSGLGPRYV DYVLGIVKAY STRVGAGPFP TELNDETGEF LRKQGNEYGA
TTGRSRRTGW LDIVAVRRAV QINSLSGFCM TKLDVLDGLK EVKLCIGYRM PDGREVDTTP
LAAEGWEGIE PIYETMPGWS ETTFGVKEHS KLPQAALNYI QRVEELTGVP IDIISTGPDR
DETMILRDPF DA
