ID DHAS_ECOL6 Reviewed; 367 AA. AC Q8FCR6; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2004, sequence version 2. DT 16-JUN-2009, entry version 45. DE RecName: Full=Aspartate-semialdehyde dehydrogenase; DE Short=ASA dehydrogenase; DE Short=ASADH; DE EC=1.2.1.11; GN Name=asd; OrderedLocusNames=c4220; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). 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; AE014075; AAN82658.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_756084.2; -. DR HSSP; P00353; 1GL3. DR SMR; Q8FCR6; 1-367. DR GeneID; 1036947; -. DR GenomeReviews; AE014075_GR; c4220. DR KEGG; ecc:c4220; -. DR HOGENOM; Q8FCR6; -. DR OMA; Q8FCR6; IDGLCVR. DR BRENDA; 1.2.1.11; 292881. 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR011534; Asp_ADH_proteob. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_C. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR TIGRFAMs; TIGR01745; asd_gamma; 1. DR PROSITE; PS01103; ASD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; KW Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; KW Oxidoreductase. FT CHAIN 1 367 Aspartate-semialdehyde dehydrogenase. FT /FTId=PRO_0000141371. FT ACT_SITE 135 135 Acyl-thioester intermediate (By FT similarity). FT BINDING 135 135 Cysteine (covalent); in inhibited form FT (By similarity). SQ SEQUENCE 367 AA; 40031 MW; 33EDFC97960D14D6 CRC64; MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQL GQAAPSFGGT TGTLQDAFDL EALKALDIIV TCQGGDYTNE IYPKLRESGW QGYWIDAASS LRMKDDAIII LDPVNQDVIT DGLNNGIRTF VGGNCTVSLM LMSLGGLFAN DLVDWVSVAT YQAASGGGAR HMRELLTQMG HLYGHVADEL ANPSSAILDI ERKVTTLTRS GELPVDNFGV PLAGSLIPWI DKQLDNGQSR EEWKGQAETN KILNTSSVIP VDGLCVRVGA LRCHSQAFTI KLKKDVSIPT VEELLAAHNP WAKVVPNDRE ITMRELTPAA VTGTLTTPVG RLRKLNMGPE FLSAFTVGDQ LLWGAAEPLR RMLRQLA //