ID A0A2N0LEQ0_9CHLR Unreviewed; 340 AA. AC A0A2N0LEQ0; 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 ORFNames=BZY82_00660 {ECO:0000313|EMBL:PKB68530.1}; OS SAR202 cluster bacterium Io17-Chloro-G3. OC Bacteria; Chloroflexi; SAR202 cluster. OX NCBI_TaxID=1926612 {ECO:0000313|EMBL:PKB68530.1}; RN [1] {ECO:0000313|EMBL:PKB68530.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Io17-Chloro-G3 {ECO:0000313|EMBL:PKB68530.1}; RX PubMed=29208946; RA Mehrshad M., Rodriguez-Valera F., Amoozegar M.A., Lopez-Garcia P., RA Ghai R.; RT "The enigmatic SAR202 cluster up close: shedding light on a globally RT distributed dark ocean lineage involved in sulfur cycling."; RL ISME J. 0:0-0(2017). 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:PKB68530.1}. 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; MUCQ01000003; PKB68530.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. 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; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. 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 SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01296; asd_B; 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 5 120 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. FT NP_BIND 12 15 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 40 41 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 129 129 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 242 242 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 100 100 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 156 156 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 235 235 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. SQ SEQUENCE 340 AA; 37137 MW; FD1EE4C704B16CB4 CRC64; MSDLNVAVVG ATGLVGSEFL RILEHWTVPI KSLSLYASDR SAGTPLQFQG SDLRVEETSD DSFKGIDIAL FSAGADVSER FAPVAVRSGA VVVDNSSAFR MDPDAPLVIP EVNPNDLEKH QGIIANPNCS TIQMLVALYP LHQINPIKRI IVSTYQAVAG TGTAAVDELN QQIRQVMEGE KTSPKVYPHQ IAFNVIPFVD DFLDNGYTVE EWKMVSETRK ILHLPDMPVS ATCVRVPVYL SHSEAVNVEL SNPMSPEEAR EVLSRAPGVE VVDDPANQMY PLALTATGRD EVFVGRVREG LSHPNSLAMW IVADDLRKGA ALNAVQIAEE ILRRNLLLSR //