(data stored in ACNUC7421 zone)

SWISSPROT: 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   07-JUN-2017, entry version 117.
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=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;
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: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-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-
CC       Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP 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}.
DR   EMBL; AF026490; AAB86714.1; -; Genomic_DNA.
DR   EMBL; CP001600; ACR67653.1; -; Genomic_DNA.
DR   RefSeq; WP_015869857.1; NC_012779.2.
DR   SMR; O31047; -.
DR   STRING; 634503.NT01EI_0415; -.
DR   PRIDE; O31047; -.
DR   EnsemblBacteria; ACR67653; ACR67653; NT01EI_0415.
DR   GeneID; 7961240; -.
DR   KEGG; eic:NT01EI_0415; -.
DR   PATRIC; fig|634503.3.peg.375; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; GVSKAYT; -.
DR   OrthoDB; POG091H01G9; -.
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-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03108; AdSS; 1.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR   InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
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;
DR   PRODOM; O31047.
DR   SWISS-2DPAGE; O31047.
KW   Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    432       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000095177.
FT   NP_BIND      13     19       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND      41     43       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND     332    334       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND     415    417       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   REGION       14     17       IMP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   REGION       39     42       IMP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   REGION      300    306       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     14     14       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     42     42       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   METAL        14     14       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   METAL        41     41       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     130    130       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     144    144       IMP; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     225    225       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     240    240       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     304    304       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     306    306       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   CONFLICT    259    259       C -> R (in Ref. 1; AAB86714).
FT                                {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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