ID A0A059G6K2_9RHOB Unreviewed; 347 AA. AC A0A059G6K2; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 27-MAY-2015, entry version 8. 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 ORFNames=HOC_11333 {ECO:0000313|EMBL:KDA02349.1}; OS Hyphomonas oceanitis SCH89. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=1280953 {ECO:0000313|EMBL:KDA02349.1}; RN [1] {ECO:0000313|EMBL:KDA02349.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCH89 {ECO:0000313|EMBL:KDA02349.1}; RX PubMed=25070064; DOI=10.1007/s10482-014-0236-y; RA Li C., Lai Q., Li G., Dong C., Wang J., Liao Y., Shao Z.; RT "Hyphomonas beringensis sp. nov. and Hyphomonas chukchiensis sp. nov., RT isolated from surface seawater of the Bering Sea and Chukchi Sea."; RL Antonie Van Leeuwenhoek 106:657-665(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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDA02349.1}. 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; ARYL01000015; KDA02349.1; -; Genomic_DNA. DR RefSeq; WP_035538553.1; NZ_ARYL01000015.1. DR EnsemblBacteria; KDA02349; KDA02349; HOC_11333. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. 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 TIGRFAMs; TIGR01296; asd_B; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; 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:0000256|HAMAP-Rule:MF_02121}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121}; KW Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 11 14 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 39 40 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 160 161 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 130 130 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121, FT ECO:0000256|PIRSR:PIRSR000148-1}. FT ACT_SITE 242 242 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121, ECO:0000256|PIRSR:PIRSR000148- FT 1}. FT BINDING 99 99 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 157 157 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 235 235 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 315 315 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 347 AA; 37853 MW; 6A7FE08257D57851 CRC64; MATRIAVVGA TGNVGRELLN ILDERLFPAD EVFAVASRRS IGKEVSYGDK TLKCHDLESF DFKRVDLVLM SAGGTISKLW APKIAAAGAI VIDNSSAWRM DKDVPLVVPE VNADAVMGYA KKNIIANPNC STAQLVVALK PIHDAVGITR VVVATYQSVS GAGKDGMDEL WNQTKGIFVN DEPTPQVFQK DIAFNVIPQI DVFMDDGFTK EEWKMREETK KILDPAIELV ATCVRVPVFV GHSEAVHIEM AGPMSAAEAK RLLRESPGIM LVDDPKEELY ITPKECVGDW ATFISRVRKD PTVENGLAFW CVSDNLRKGA ALNAVQIAEE LLNRGVLKAE KQAVTTG //