(data stored in ACNUC1104 zone)

SWISSPROT: D3UYU7_XENBS

ID   D3UYU7_XENBS            Unreviewed;       432 AA.
AC   D3UYU7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE            Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_00011};
DE            Short=AdSS {ECO:0000256|HAMAP-Rule:MF_00011};
DE            EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE   AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011};
GN   Name=purA {ECO:0000256|HAMAP-Rule:MF_00011,
GN   ECO:0000313|EMBL:CBJ79475.1};
GN   OrderedLocusNames=XBJ1_0325 {ECO:0000313|EMBL:CBJ79475.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79475.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79475.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79475.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00011};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011,
CC       ECO:0000256|RuleBase:RU000520}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}.
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DR   EMBL; FN667741; CBJ79475.1; -; Genomic_DNA.
DR   RefSeq; WP_012986935.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0325; -.
DR   EnsemblBacteria; CBJ79475; CBJ79475; XBJ1_0325.
DR   GeneID; 8829950; -.
DR   KEGG; xbo:XBJ1_0325; -.
DR   PATRIC; fig|406818.4.peg.297; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; SNAGHTV; -.
DR   BioCyc; XBOV406818:XBJ1_RS01415-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000002045; 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;
DR   PRODOM; D3UYU7.
DR   SWISS-2DPAGE; D3UYU7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520, ECO:0000313|EMBL:CBJ79475.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   NP_BIND      13     19       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND      41     43       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     332    334       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     415    417       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   REGION       14     17       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION       39     42       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION      300    306       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     14     14       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE     42     42       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE    141    141       {ECO:0000256|PROSITE-ProRule:PRU10134}.
FT   METAL        14     14       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   METAL        41     41       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     130    130       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     144    144       IMP; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     225    225       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     240    240       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     304    304       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     306    306       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
SQ   SEQUENCE   432 AA;  47179 MW;  26FCBA1FE4F774AB CRC64;
     MGKNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI
     LRENVISIIA NGVVLAPDAL MKEMNALESR GIPVRERLLI SEACPLILPY HVALDNAREK
     ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFDKETFAV KLQEIIEYHN FQLVNYYNEP
     AVDYQKTLDD ILAVADILTN MVVDVSDLLY KATQKGELVM FEGAQGTLLD IDHGTYPYVT
     SSNTTAGGVA TGSGLGPRYV DYVLGIIKAY STRVGAGPFP TELFDETGEY LRQKGQEFGA
     TTGRSRRTGW LDIVAIRRAI QINSLSGFCM TKLDVLDGLK EVKVCIGYRM PDGSVIDTTP
     LAAENWEGLE AVYETLPGWD ESTFGVKDHS LLPEAALSYI KRVEELTGVP VDIISTGPDR
     AETMILRDPF DA
//

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