ID D3DYW9_METRM Unreviewed; 349 AA. AC D3DYW9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 05-OCT-2010, entry version 7. DE RecName: Full=Aspartate-semialdehyde dehydrogenase; DE EC=1.2.1.11; GN Name=asd; OrderedLocusNames=mru_1669; OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM OS 13430 / M1) (Methanobacterium ruminantium). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=634498; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20126622; DOI=10.1371/journal.pone.0008926; RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J., RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C., RA Janssen P.H., Dey D., Attwood G.T.; RT "The genome sequence of the rumen methanogen Methanobrevibacter RT ruminantium reveals new possibilities for controlling ruminant methane RT emissions."; RL PLoS ONE 5:E8926-E8926(2010). 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 -!- 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; CP001719; ADC47519.1; -; Genomic_DNA. DR RefSeq; YP_003424411.1; -. DR GeneID; 8771331; -. DR GenomeReviews; CP001719_GR; mru_1669. DR KEGG; mru:mru_1669; -. 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: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; IPR005676; Asp_semi-ald_DH_pep-lack. DR InterPro; IPR012080; Asp_semialdehyde_DH. 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; TIGR00978; asd_EA; 1. DR PROSITE; PS01103; ASD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; NADP; Oxidoreductase. FT ACT_SITE 148 148 Acyl-thioester intermediate (By FT similarity). SQ SEQUENCE 349 AA; 38336 MW; 30B76E17D60ABB69 CRC64; MVKVGVLGAT GMVGQRFIQL LADHPDFEIA ALAASSRSAG KKYEDATTWY MNDEMPESVR DIKVIETDPA HMDKDVEIVF SSLPADFAAK VEPEYAKDFV VASNASAMRM KKDIPLVIPE VNPQFLDMIE AQQKNNNWDG FIVTNPNCST IALTLTLKPI YDNFNINRIY VSTMQAVSGA GYNGVPSMAI LDNLVPYIGG EEEKMESETL HLLGSLDGDE VVPANFSLSA SCHRVPVIDG HTEAVFVELD EEADIDKIKK TMADFRGLPQ ELGLHSAPEQ PVIVKEEDDR PQPRMDRMAY GGMAATVGRL RKDQAFDNSF KYVLVGHNTI RGAAGASILN AELINKQIL //