ID DHAS_SHEVI Reviewed; 338 AA. AC Q56734; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=Aspartate-semialdehyde dehydrogenase; DE Short=ASA dehydrogenase; DE Short=ASADH; DE EC=1.2.1.11; GN Name=asd; OS Shewanella violacea. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60217; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSS12; RX MEDLINE=97306055; PubMed=9163523; RA Kato C., Smorawinska M., Li L., Horikoshi K.; RT "Comparison of the gene expression of aspartate beta-D-semialdehyde RT dehydrogenase at elevated hydrostatic pressure in deep-sea bacteria."; RL J. Biochem. 121:717-723(1997). 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; D49540; BAA08490.1; -; Genomic_DNA. DR PIR; JC5436; JC5436. DR HSSP; P00353; 1BRM. DR BRENDA; 1.2.1.11; 292658. 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 1 338 Aspartate-semialdehyde dehydrogenase. FT /FTId=PRO_0000141390. FT ACT_SITE 132 132 Acyl-thioester intermediate (By FT similarity). SQ SEQUENCE 338 AA; 37061 MW; 8D0DC1F46EAF30AC CRC64; MSQEFNVVVL GASGAVGQTM IEILEERNFP VAKLFPLASS RSAGGTVSFN GKQVEILDVD DFDWSQAQIG FFSAGGDVSE KWAPIAAENG CVVIDNTSQF RYDNDVPLVI PEVNPEAIAD FRNRNIIANP NCSTIQMLVA LKPIYDAFGI SRINVATYQS VSGSGKEAIT ELAGQCSKLL HGLPAESKVY PKQIAFNVLP QIDKFMENGY TKEEMKMVWE TQKIFGDDNI VVNPTAVRVP VFYGHSEAIH LETIQPAEAE DVKAVLREAP GIELFESNEE YPTAVTESAG TDPVYVGRVR KDISHSHGIN LWVVSDNIRK GAALNSVQIA EVLIRDYY //