ID A0A2Z6AYH1_9DELT Unreviewed; 344 AA. AC A0A2Z6AYH1; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 08-MAY-2019, entry version 7. 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=DFE_1542 {ECO:0000313|EMBL:BBD08268.1}; OS Desulfovibrio ferrophilus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=241368 {ECO:0000313|EMBL:BBD08268.1, ECO:0000313|Proteomes:UP000269883}; RN [1] {ECO:0000313|EMBL:BBD08268.1, ECO:0000313|Proteomes:UP000269883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IS5 {ECO:0000313|EMBL:BBD08268.1, RC ECO:0000313|Proteomes:UP000269883}; RX PubMed=29464208; DOI=10.1126/sciadv.aao5682; RA Deng X., Dohmae N., Nealson K.H., Hashimoto K., Okamoto A.; RT "Multi-heme cytochromes provide a pathway for survival in energy- RT limited environments."; RL Sci. Adv. 4:eaao5682-eaao5682(2018). 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 --------------------------------------------------------------------------- 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; AP017378; BBD08268.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000269883; Chromosome. 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; 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Complete proteome {ECO:0000313|Proteomes:UP000269883}; 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 7 122 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. FT NP_BIND 14 17 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 42 43 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 161 162 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 131 131 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 246 246 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 102 102 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 158 158 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 239 239 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 319 319 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 344 AA; 37420 MW; CD3CC44AE16BDBAB CRC64; MAKEGYVVAV CGATGAVGRT MLEVLEQRDF PASKVIALAS ERSAGKKVPF KGGELTVEVL NEYSFEGVDL ALFSAGGSTS KTFAPLAAKA GCVVVDNSSA WRMDPECPLV VPEVNPHDLE WHKGIIANPN CSTIQMMVAL KPIHDAAKIK RVVVSTYQAV SGTGQKAIDE LAGQVTMMFN GQVEDIEPSA YPHRIAFNCL PHIDIFMDND YTREEMKMVH ETTKIMGDES IKVTATAVRV PVFYGHSESI NIETELKLSA KECRALLTQA PGVQVLDNPA EQIYPMPIEA QGQDATYVGR IREDETIANG LNIWVVSDNI RKGAATNTVQ IAEKLIEMDL VRVP //