ID Q8DQ00_STRR6 Unreviewed; 358 AA. AC Q8DQ00; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; DE Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11 {ECO:0000256|HAMAP-Rule:MF_02121}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000256|HAMAP-Rule:MF_02121, GN ECO:0000313|EMBL:AAK99722.1}; GN OrderedLocusNames=spr0918 {ECO:0000313|EMBL:AAK99722.1}; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99722.1, ECO:0000313|Proteomes:UP000000586}; RN [1] {ECO:0000213|PDB:3Q1L} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RX PubMed=22039970; DOI=10.1111/j.1747-0285.2011.01267.x; RA Pavlovsky A.G., Liu X., Faehnle C.R., Potente N., Viola R.E.; RT "Structural characterization of inhibitors with selectivity against RT members of a homologous enzyme family."; RL Chem. Biol. Drug Des. 79:128-136(2012). RN [2] {ECO:0000213|PDB:4R3N} RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH NADP. RX PubMed=25478842; DOI=10.1107/S1399004714023979; RA Pavlovsky A.G., Thangavelu B., Bhansali P., Viola R.E.; RT "A cautionary tale of structure-guided inhibitor development against RT an essential enzyme in the aspartate-biosynthetic pathway."; RL Acta Crystallogr. D 70:3244-3252(2014). CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_02121, CC ECO:0000256|RuleBase:RU004041}. 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; AE007317; AAK99722.1; -; Genomic_DNA. DR PIR; F97986; F97986. DR RefSeq; NP_358512.1; NC_003098.1. DR RefSeq; WP_000542475.1; NC_003098.1. DR PDB; 3Q1L; X-ray; 2.30 A; A/B/C/D=1-358. DR PDB; 4R3N; X-ray; 1.35 A; A/B=1-358. DR PDBsum; 3Q1L; -. DR PDBsum; 4R3N; -. DR ProteinModelPortal; Q8DQ00; -. DR SMR; Q8DQ00; 2-358. DR STRING; 171101.spr0918; -. DR EnsemblBacteria; AAK99722; AAK99722; spr0918. DR GeneID; 933797; -. DR KEGG; spr:spr0918; -. DR PATRIC; 19701775; VBIStrPne107296_1005. DR eggNOG; COG0136; LUCA. DR eggNOG; ENOG4105CM3; Bacteria. DR HOGENOM; HOG000013357; -. DR KO; K00133; -. DR OMA; KWHKGII; -. DR OrthoDB; EOG6JB158; -. DR BioCyc; SPNE171101:GJC8-930-MONOMER; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000000586; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01296; asd_B; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3Q1L, ECO:0000213|PDB:4R3N}; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Complete proteome {ECO:0000313|Proteomes:UP000000586}; KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW NADP {ECO:0000213|PDB:4R3N, ECO:0000256|HAMAP-Rule:MF_02121}; KW Nucleotide-binding {ECO:0000213|PDB:4R3N}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121, KW ECO:0000313|EMBL:AAK99722.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000586}; KW Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}. FT DOMAIN 4 119 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. FT NP_BIND 9 14 NADP. {ECO:0000213|PDB:4R3N}. FT NP_BIND 11 14 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 36 40 NADP. {ECO:0000213|PDB:4R3N}. FT NP_BIND 39 40 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 126 128 NADP. {ECO:0000213|PDB:4R3N}. FT NP_BIND 158 159 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 162 163 NADP. {ECO:0000213|PDB:4R3N}. FT ACT_SITE 128 128 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121, FT ECO:0000256|PIRSR:PIRSR000148-1}. FT ACT_SITE 252 252 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121, ECO:0000256|PIRSR:PIRSR000148- FT 1}. FT BINDING 71 71 NADP. {ECO:0000213|PDB:4R3N}. FT BINDING 94 94 NADP. {ECO:0000213|PDB:4R3N}. FT BINDING 99 99 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 155 155 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 245 245 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 325 325 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT BINDING 329 329 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:4R3N}. SQ SEQUENCE 358 AA; 38924 MW; 366715956847C96C CRC64; MGYTVAVVGA TGAVGAQMIK MLEESTLPID KIRYLASARS AGKSLKFKDQ DITIEETTET AFEGVDIALF SAGSSTSAKY APYAVKAGVV VVDNTSYFRQ NPDVPLVVPE VNAHALDAHN GIIACPNCST IQMMVALEPV RQKWGLDRII VSTYQAVSGA GMGAILETQR ELREVLNDGV KPCDLHAEIL PSGGDKKHYP IAFNALPQID VFTDNDYTYE EMKMTKETKK IMEDDSIAVS ATCVRIPVLS AHSESVYIET KEVAPIEEVK AAIAAFPGAV LEDDVAHQIY PQAINAVGSR DTFVGRIRKD LDAEKGIHMW VVSDNLLKGA AWNSVQIAET LHERGLVRPT AELKFELK //