ID A0A3D9DQJ5_9FLAO Unreviewed; 330 AA. AC A0A3D9DQJ5; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 03-AUG-2022, entry version 9. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120, 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|ARBA:ARBA00013120, 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; Weeksellaceae; OC Chryseobacterium group; 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., Park K.H., RA Kim S.B.; RT "Four new species of Chryseobacterium from the rhizosphere of coastal sand RT dune plants, Chryseobacterium elymi sp. nov., Chryseobacterium hagamense RT sp. nov., Chryseobacterium lathyri sp. nov. and Chryseobacterium RT 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-aspartyl- CC 4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho- CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; CC Evidence={ECO:0000256|ARBA:ARBA00001636, 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|ARBA:ARBA00005076, ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000256|ARBA:ARBA00005021, ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097, CC ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00010584, ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 EnsemblBacteria; REC80259; REC80259; DRF60_00650. 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-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule. 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 Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915, KW ECO:0000256|HAMAP-Rule:MF_02121}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP- KW Rule:MF_02121}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_02121}; 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|ARBA:ARBA00022697, ECO:0000256|HAMAP- KW Rule:MF_02121}. FT DOMAIN 2..117 FT /note="Semialdhyde_dh" FT /evidence="ECO:0000259|SMART:SM00859" FT ACT_SITE 126 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 235 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 9..12 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 37..38 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 97 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 228 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 308 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="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 //