ID D0U4N0_9GAMM Unreviewed; 341 AA. AC D0U4N0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 09-JAN-2013, entry version 21. DE RecName: Full=Aspartate-semialdehyde dehydrogenase; DE Short=ASA dehydrogenase; DE Short=ASADH; DE EC=1.2.1.11; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase; GN Name=asd; ORFNames=Sup05_1334, SUP05_FGYC65E210007; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillales; SUP05 cluster; environmental samples. OX NCBI_TaxID=655186; RN [1] RP NUCLEOTIDE SEQUENCE. RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oxygen RT minimum zones."; RL Science 326:578-582(2009). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.G., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic RT dead zones."; RL Science 326:578-582(2009). CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate (By similarity). 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; (S)-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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GQ351269; ACX30562.1; -; Genomic_DNA. DR EMBL; GG730003; EEZ80090.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:HAMAP. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:HAMAP. DR Gene3D; 3.40.50.720; NAD(P)-bd; 1. DR HAMAP; MF_02121; ASADH; 1; -. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR016040; NAD(P)-bd_dom. 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 PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR TIGRFAMs; TIGR01296; asd_B; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; KW Lysine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase; KW Threonine biosynthesis. FT NP_BIND 13 16 NADP (By similarity). FT NP_BIND 41 42 NADP (By similarity). FT NP_BIND 162 163 NADP (By similarity). FT ACT_SITE 132 132 Acyl-thioester intermediate (By FT similarity). FT ACT_SITE 246 246 Proton acceptor (By similarity). FT BINDING 101 101 Phosphate (By similarity). FT BINDING 159 159 Substrate (By similarity). FT BINDING 239 239 Substrate (By similarity). FT BINDING 320 320 NADP (By similarity). SQ SEQUENCE 341 AA; 37274 MW; 79A54BF5014C0711 CRC64; MSKKYNVAVV GATGAVGETI LSILEQRNFP IDNLYPLASA NSAGKKVFCQ GKSWTVQDLD TFDFSQAQIG LFSAGGNISE KYAPIAAEAG CVVIDNTAHF RRDEGIPLVV PEVNPHAISG YTKRNIIANP NCSTIQMLVA LKPIYDAVGI ERINVATYQA VSGSGKEAIS ELIEQTTKLL GGNTEVDVEV YPKQIAFNVI PHIDVFQDNG YTKEEMKMVW ETQKIFEDDN ILVNPTAVRV PVIYGHSEAI NIETKTKITA AEAVEVLSKA NGVTVLDKRE DGGYATPFVE ATNHDDTFVS RIREDISHEK GLNLWVVSDN IRKGAALNSI QIAEILIEEY L //