ID A0A0M7D0W2_ALCFA Unreviewed; 374 AA. AC A0A0M7D0W2; A0A0S2JLW0; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 13-FEB-2019, entry version 23. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; DE Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11 {ECO:0000256|HAMAP-Rule:MF_02121}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000256|HAMAP-Rule:MF_02121, GN ECO:0000313|EMBL:PWE15907.1}; GN ORFNames=DF183_04050 {ECO:0000313|EMBL:PWE15907.1}; OS Alcaligenes faecalis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Alcaligenes. OX NCBI_TaxID=511 {ECO:0000313|EMBL:PWE15907.1, ECO:0000313|Proteomes:UP000245216}; RN [1] {ECO:0000313|EMBL:PWE15907.1, ECO:0000313|Proteomes:UP000245216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YBY {ECO:0000313|EMBL:PWE15907.1, RC ECO:0000313|Proteomes:UP000245216}; RA Yang B.; RT "Genome Sequence of an Efficient Indole-Degrading Bacterium, RT Alcaligenes sp.YBY."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:PWE15907.1, ECO:0000313|Proteomes:UP000245216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YBY {ECO:0000313|EMBL:PWE15907.1, RC ECO:0000313|Proteomes:UP000245216}; RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., RA Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Rusch D., RA Podicherti R., Tsui H.-C.T., Winkler M.E.; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4- CC phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; CC EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_02121, CC ECO:0000256|SAAS:SAAS00827794}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PWE15907.1}. 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; QEXO01000001; PWE15907.1; -; Genomic_DNA. DR RefSeq; WP_042481031.1; NZ_QEXO01000001.1. DR EnsemblBacteria; CUI45919; CUI45919; ERS370012_00998. DR GeneID; 29371425; -. DR KEGG; afa:UZ73_01020; -. DR KO; K00133; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000245216; Unassembled WGS sequence. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR011534; Asp_ADH_gamma-type. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR PANTHER; PTHR10174:SF116; PTHR10174:SF116; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01745; asd_gamma; 1. DR PROSITE; PS01103; ASD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Complete proteome {ECO:0000313|Proteomes:UP000245216}; KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW NADP {ECO:0000256|HAMAP-Rule:MF_02121}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121}; KW Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 11 14 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 166 167 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 136 136 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 278 278 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 74 74 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT BINDING 103 103 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 163 163 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 242 242 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 245 245 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 271 271 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 354 354 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 374 AA; 40245 MW; A797987FFF8B1BFD CRC64; MTQAVGLVGW RGMVGSVLMQ RMRDEGDFSL FQPVFFSTSN AGGAAPSWAD GAGPLQDAHD IDALKKLPII VTAQGGDYTS QIYPKLRAAG WNGLWIDAAS TLRMDENSVI VLDPINRPVI DAALAKGGKQ FIGGNCTVSC MLMGLGGLFN QNLVEWMTSM TYQAASGGGA QHMRELLTQF GLINQSVSSL LDDPASAILD IDRGVLQTQR DPNLPQKNFG VPLGGSLIPW IDSDLGNGMT REEWKAGVET NKILGRGAQD KHIPIDGLCV RIGAMRCHSQ ALTIKLTRDV PLDEITDILA EGSKWAKVVP NERQATVEAL TPVAVTGTLD IPVGRLRKLN MGPEYLSAFT VGDQLLWGAA EPLRRMLRIA LGEL //