ID A0A2N4U3C2_9BURK Unreviewed; 376 AA. AC A0A2N4U3C2; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 13-FEB-2019, entry version 6. 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:PLC49497.1}; GN ORFNames=CR159_12905 {ECO:0000313|EMBL:PLC49497.1}; OS Pusillimonas sp. JR1/69-3-13. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Pusillimonas. OX NCBI_TaxID=2045210 {ECO:0000313|EMBL:PLC49497.1, ECO:0000313|Proteomes:UP000234190}; RN [1] {ECO:0000313|EMBL:PLC49497.1, ECO:0000313|Proteomes:UP000234190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JR1/69-3-13 {ECO:0000313|EMBL:PLC49497.1, RC ECO:0000313|Proteomes:UP000234190}; RA Grouzdev D.S., Tourova T.P., Goeva M.A., Babich T.L., Sokolova D.S., RA Abdullin R., Poltaraus A.B., Toshchakov S.V., Nazina T.N.; RT "Two draft genome sequences of Pusillimonas sp. strains isolated from RT a nitrate- and radionuclide-contaminated groundwater in Russia."; RL Submitted (OCT-2017) 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:PLC49497.1}. 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; PDNW01000010; PLC49497.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000234190; 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:UP000234190}; 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 DOMAIN 4 123 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. 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 280 280 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 273 273 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 356 356 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 376 AA; 40723 MW; D8FEBD82DE9B6049 CRC64; MNQVVGLVGW RGMVGSVLMQ RMRDENDFSL FEPVFFSTSN AGGAAPAWAE GAGPLQDAYD IDALKKLPII LTAQGGDYTS AVYPKLRAAG WPGVWIDAAS TLRMADDAII VLDPVNRPVI DAALERGVKN FVGGNCTVSC MLMGLSGLFN NDLIEWMSSM TYQAASGGGA QHMRELLTQF GALNAAVKLQ LDDPASAILD IDRGVLNMQQ DPNLPREHFG VPLGGNLIPW IDKDLGNGMS REEWKAEAET NKILGRGAAF GTAPTPIDGL CVRIGAMRCH SQALTIKLKR DVPLDEISDM LREGSEWAKV IPNERDITMQ QLTPVAVTGT LDIPVGRLRK MSMGPEYLSA FTVGDQLLWG AAEPLRRMLR ITLGEL //