ID D3DYW9_METRM Unreviewed; 349 AA. AC D3DYW9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 11-JUN-2014, entry version 33. 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; 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]. RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / M1; 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 -!- 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; CP001719; ADC47519.1; -; Genomic_DNA. DR RefSeq; YP_003424411.1; NC_013790.1. DR ProteinModelPortal; D3DYW9; -. DR EnsemblBacteria; ADC47519; ADC47519; mru_1669. DR GeneID; 8771331; -. DR KEGG; mru:mru_1669; -. DR HOGENOM; HOG000013358; -. DR KO; K00133; -. DR OMA; MSIVVGR; -. DR BioCyc; MRUM634498:GHDG-1714-MONOMER; -. 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:UniProtKB-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:UniProtKB-HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR005676; Asp_semi-ald_DH_pep-lack. 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_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; KW Diaminopimelate biosynthesis; Lysine biosynthesis; KW Methionine biosynthesis; NADP; Oxidoreductase; Threonine biosynthesis. FT NP_BIND 10 13 NADP (By similarity){EA7}. FT NP_BIND 37 38 NADP (By similarity){EA7}. FT NP_BIND 178 179 NADP (By similarity){EA7}. FT NP_BIND 328 329 NADP (By similarity){EA7}. FT ACT_SITE 148 148 Acyl-thioester intermediate (By FT similarity){EA7,EA8}. FT ACT_SITE 241 241 Proton acceptor (By similarity){EA7,EA8}. FT BINDING 109 109 Phosphate (By similarity){EA7}. FT BINDING 175 175 Substrate (By similarity){EA7}. FT BINDING 201 201 Substrate (By similarity){EA7}. FT BINDING 204 204 Phosphate (By similarity){EA7}. FT BINDING 234 234 Substrate (By similarity){EA7}. 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 //