ID L0CEG4_ECOLX Unreviewed; 158 AA. AC L0CEG4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 29-SEP-2021, entry version 36. DE SubName: Full=Adenylosuccinate dehydrogenase {ECO:0000313|EMBL:AGA13695.1}; DE Flags: Fragment; GN Name=purA {ECO:0000313|EMBL:AGA13695.1}; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:AGA13695.1}; RN [1] {ECO:0000313|EMBL:AGA13695.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3662 {ECO:0000313|EMBL:AGA13699.1}, 3665 RC {ECO:0000313|EMBL:AGA13702.1}, 3677 {ECO:0000313|EMBL:AGA13704.1}, and RC 3697 {ECO:0000313|EMBL:AGA13695.1}; RX PubMed=22995280; DOI=10.1016/j.meegid.2012.09.003; RA Gonzalez-Gonzalez A., Sanchez-Reyes L.L., Delgado Sapien G., Eguiarte L.E., RA Souza V.; RT "Hierarchical clustering of genetic diversity associated to different RT levels of mutation and recombination in Escherichia coli: A study based on RT Mexican isolates."; RL Infect. Genet. Evol. 13C:187-197(2012). RN [2] {ECO:0000313|EMBL:AGA13695.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3662 {ECO:0000313|EMBL:AGA13699.1}, 3665 RC {ECO:0000313|EMBL:AGA13702.1}, 3677 {ECO:0000313|EMBL:AGA13704.1}, and RC 3697 {ECO:0000313|EMBL:AGA13695.1}; RA Gonzalez A.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AIQ87494.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR54 {ECO:0000313|EMBL:AIQ87494.1}, and PR56 RC {ECO:0000313|EMBL:AIQ87496.1}; RA Rakov A.V., Wang X.-Y., Wang C.-X., Liu S.-L.; RT "Genetic boundaries delineating Escherichia coli into genetic clusters of RT bacteria."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JQ819070; AGA13695.1; -; Genomic_DNA. DR EMBL; JQ819074; AGA13699.1; -; Genomic_DNA. DR EMBL; JQ819077; AGA13702.1; -; Genomic_DNA. DR EMBL; JQ819079; AGA13704.1; -; Genomic_DNA. DR EMBL; KM072714; AIQ87494.1; -; Genomic_DNA. DR EMBL; KM072716; AIQ87496.1; -; Genomic_DNA. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.300.10; -; 1. DR Gene3D; 3.40.440.10; -; 1. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS. DR InterPro; IPR042109; Adenylosuccinate_synth_dom1. DR InterPro; IPR042110; Adenylosuccinate_synth_dom2. 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 PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}. FT ACT_SITE 26 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGA13695.1" FT NON_TER 158 FT /evidence="ECO:0000313|EMBL:AGA13695.1" SQ SEQUENCE 158 AA; 17285 MW; C4F7CC1C3092A0FD CRC64; NAREKARGAK AIGTTGRGIG PAYEDKVARR GLRVGDLFDK ETFAEKLKEV MEYHNFQLVN YYNAEAVDYQ KVLDDTMAVA DILTSMVVDV SDLLDQARQR GDFVMFEGAQ GTLLDIDHGT YPYVTSSNTT AGGVATGSGL GPRYVDYVLG ILKAYSTR //