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PURA_EDWI9
ID   PURA_EDWI9              Reviewed;         432 AA.
AC   O31047; C5BF67;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 4.
DT   03-AUG-2022, entry version 147.
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}; OrderedLocusNames=NT01EI_0415;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9353045; DOI=10.1128/iai.65.11.4642-4651.1997;
RA   Lawrence M.L., Cooper R.K., Thune R.L.;
RT   "Attenuation, persistence, and vaccine potential of an Edwardsiella
RT   ictaluri purA mutant.";
RL   Infect. Immun. 65:4642-4651(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AF026490; AAB86714.1; -; Genomic_DNA.
DR   EMBL; CP001600; ACR67653.1; -; Genomic_DNA.
DR   RefSeq; WP_015869857.1; NC_012779.2.
DR   AlphaFoldDB; O31047; -.
DR   SMR; O31047; -.
DR   STRING; 67780.B6E78_12850; -.
DR   EnsemblBacteria; ACR67653; ACR67653; NT01EI_0415.
DR   GeneID; 7961240; -.
DR   KEGG; eic:NT01EI_0415; -.
DR   PATRIC; fig|634503.3.peg.375; -.
DR   HOGENOM; CLU_029848_0_0_6; -.
DR   OMA; FHHAKPI; -.
DR   OrthoDB; 232152at2; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000001485; 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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..432
FT                   /note="Adenylosuccinate synthetase"
FT                   /id="PRO_0000095177"
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"
FT   CONFLICT        259
FT                   /note="C -> R (in Ref. 1; AAB86714)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   432 AA;  47033 MW;  459914300E7D5AE9 CRC64;
     MGKNVVVLGT QWGDEGKGKV VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI
     LRENVVSIIA NGVVLAPDAL LREMTELEAR GVPVRERLLL SEACPLILPY HVALDNAREK
     ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFDKASFAV KLKEIMEYHN FQLVNYYHVD
     AVDYQSVLDE VMAVADLLTS MVVDVADLLN KAYRNGEYVM FEGAQGTLLD IDHGTYPYVT
     SSNTTAGGVA TGSGIGPRCV DYVLGIVKAY STRVGAGPFP TELFDSVGEF LCEKGNEFGA
     TTGRRRRTGW LDAVAVRRAV ELNSLSGFCL TKLDVLDGLD EVKICVGYRL PDGREVDVTP
     LAAEGWEGIE PIYEVLPGWK ESTFGVKLRD GLPQAALNYI KRIEEVTGVP VDIISTGPDR
     EETIVLRHPF DA
 
 
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