ID DHAS_LEGPN Reviewed; 347 AA. AC O31219; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 49. DE RecName: Full=Aspartate-semialdehyde dehydrogenase; DE Short=ASA dehydrogenase; DE Short=ASADH; DE EC=1.2.1.11; GN Name=asd; OS Legionella pneumophila. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=446; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AA100 / Serogroup 1; RX MEDLINE=98234011; PubMed=9573067; RA Harb O.S., Abu Kwaik Y.; RT "Identification of the aspartate-beta-semialdehyde dehydrogenase gene RT of Legionella pneumophila and characterization of a null mutant."; RL Infect. Immun. 66:1898-1903(1998). CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; tetrahydrodipicolinate from L-aspartate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF034213; AAC46292.1; -; Genomic_DNA. DR HSSP; P00353; 1BRM. DR BRENDA; 1.2.1.11; 1454. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:EC. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:InterPro. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_bac. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_C. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR TIGRFAMs; TIGR01296; asd_B; 1. DR PROSITE; PS01103; ASD; FALSE_NEG. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; KW Lysine biosynthesis; NADP; Oxidoreductase. FT CHAIN 1 347 Aspartate-semialdehyde dehydrogenase. FT /FTId=PRO_0000141378. FT ACT_SITE 132 132 Acyl-thioester intermediate (By FT similarity). SQ SEQUENCE 347 AA; 37714 MW; 33D992101D707943 CRC64; MSRHLNVAIV GATGAVGETF LTVLEERNFP IKSLYPLASS RSVGKTVTFR DQELDVLDLA EFDFSKVDLA LFSAGGAVSK EYAPKAVAAG CVVVDNTSCF RYEDDIPLVV PGSESSSNRD YTKRGIIANP NCSTIQMVVA LKPIYDAVGI SRINVATYQS VSGTGKKAIS ELVAQVGDLL NGRPANVQVY PQQIAFNALP HIDQFEDNGY TREEMKMVWE TRKIMEDDSI MVNPTAVRVP VIYGHSEAVH LELKKPLTAD DARALLAKAP GVTVVDNLSK ASYPTAIKNA VGHDDVFVGR IRQDISHPCG LNLWIVADNI RKGAATNAVQ IAEILQREFL LKLSLPQ //