ID A0A3D9DQJ5_9FLAO Unreviewed; 330 AA. AC A0A3D9DQJ5; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 13-FEB-2019, entry version 2. 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=DRF60_00650 {ECO:0000313|EMBL:REC80259.1}; OS Chryseobacterium elymi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=395936 {ECO:0000313|EMBL:REC80259.1, ECO:0000313|Proteomes:UP000257030}; RN [1] {ECO:0000313|EMBL:REC80259.1, ECO:0000313|Proteomes:UP000257030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 22547 {ECO:0000313|EMBL:REC80259.1, RC ECO:0000313|Proteomes:UP000257030}; RX PubMed=20185262; DOI=10.1016/j.syapm.2009.12.004; RA Cho S.H., Lee K.S., Shin D.S., Han J.H., Park K.S., Lee C.H., RA Park K.H., Kim S.B.; RT "Four new species of Chryseobacterium from the rhizosphere of coastal RT sand dune plants, Chryseobacterium elymi sp. nov., Chryseobacterium RT hagamense sp. nov., Chryseobacterium lathyri sp. nov. and RT Chryseobacterium rhizosphaerae sp. nov."; RL Syst. Appl. Microbiol. 33:122-127(2010). 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: CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4- CC phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; CC EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-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|SAAS:SAAS00827794}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}. 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:REC80259.1}. 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; QNUH01000001; REC80259.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000257030; Unassembled WGS sequence. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. 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 SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01296; asd_B; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Complete proteome {ECO:0000313|Proteomes:UP000257030}; 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 ECO:0000313|EMBL:REC80259.1}; KW Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}. FT DOMAIN 2 117 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. FT NP_BIND 9 12 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 37 38 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 126 126 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 235 235 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 97 97 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 153 153 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 228 228 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 308 308 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 330 AA; 36234 MW; ADED9837555B6305 CRC64; MKVAVVGSTG MVGQVMLKVL EERNFPVTEL IPVASERSVG KKVKYKQEEF TIVSMKDAIA AKPDIAIFSA GGSTSLEFAP LFAEAGTTVI DNSSAWRMDP TKKLVVPEIN ANVLTKEDKI IANPNCSTIQ LVMVLGPLNK KYDLKRVVVS TYQSVTGTGK AAVDQLNAEI KGDDSVAKVY PNQIFKNALP HCDVFADDDY TKEEIKLMKE PKKILGDDTF NLTATAVRVP VQGGHSESVN IEFENEFEVD EVRKILSETP GVIVLDDVKN NIYPMPLYSE GKDEVFVGRI RRDLSQPKTL NLWIVADNLR KGAATNAVQI AEYLVANNLV //