ID A0A2N4U3C2_9BURK Unreviewed; 376 AA. AC A0A2N4U3C2; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 11-DEC-2019, entry version 9. 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; unclassified 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 a RT 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-aspartyl- CC 4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho- CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; CC 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 novo CC pathway; L-homoserine from L-aspartate: step 2/3. {ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 2/5. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family. CC {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|SAAS:SAAS00827794}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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; PTHR46278:SF4; PTHR46278:SF4; 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 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 FT /note="Semialdhyde_dh" FT /evidence="ECO:0000259|SMART:SM00859" FT NP_BIND 11..14 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT NP_BIND 166..167 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 136 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 280 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 74 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 103 FT /note="Phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 163 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 242 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 245 FT /note="Phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 273 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 356 FT /note="NADP" FT /evidence="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 //