ID A0A2N1T2S3_9SPIR Unreviewed; 333 AA. AC A0A2N1T2S3; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 13-SEP-2023, entry version 15. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120, 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|ARBA:ARBA00013120, 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=CVV45_08125 {ECO:0000313|EMBL:PKL33336.1}; OS Spirochaetae bacterium HGW-Spirochaetae-10. OC Bacteria; Spirochaetota. OX NCBI_TaxID=2013833 {ECO:0000313|EMBL:PKL33336.1}; RN [1] {ECO:0000313|EMBL:PKL33336.1, ECO:0000313|Proteomes:UP000233589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HGW-Spirochaetae-10 {ECO:0000313|EMBL:PKL33336.1}; RX PubMed=28350393; DOI=10.1038/ismej.2017.39; RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K., RA Probst A., Burstein D., Thomas B.C., Banfield J.F.; RT "Potential for microbial H2 and metal transformations associated with novel RT bacteria and archaea in deep terrestrial subsurface sediments."; RL ISME J. 11:1915-1929(2017). 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|ARBA:ARBA00001636, ECO:0000256|HAMAP- CC 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|ARBA:ARBA00005076, 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. CC {ECO:0000256|ARBA:ARBA00005021, ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097, CC ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00010584, ECO:0000256|HAMAP-Rule:MF_02121}. 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:PKL33336.1}. 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; PGXX01000103; PKL33336.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2N1T2S3; -. 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR01296; asd_B; 1. DR PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915, KW ECO:0000256|HAMAP-Rule:MF_02121}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP- KW Rule:MF_02121}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_02121}; NADP {ECO:0000256|HAMAP-Rule:MF_02121}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP- KW Rule:MF_02121}. FT DOMAIN 4..119 FT /note="Semialdehyde dehydrogenase NAD-binding" FT /evidence="ECO:0000259|SMART:SM00859" FT ACT_SITE 128 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 242 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 11..14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 39..40 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 99 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 155 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 158..159 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 235 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" SQ SEQUENCE 333 AA; 35897 MW; 1AC1BC183ECAB181 CRC64; MSKNYAVVGA TGAVGVEILK VLENRNVDVG QLKLLASPRS AGKTMTFRGK EYTVEALSED SFHDVQVALF SAGGSISKQY GPVAVSSGCV VVDNSSAFRM DPEVPLVVPE INPEAVKLHK GIIANPNCST IILLMAVYPI YKLYGVKKII VSTYQAASGA GAAAMQELED QAKAHLAGTE VPTNILPHQL AFNVFSHNSS MDPESGYNQE EVKMVKETHK ILGDANIAIA PTCVRVSTFR AHAESIHLEL REKGDVEKMR EALAAFPGVK VLDNRQANRF PMPLEVSGKD DVYVGRVRMD YDDQSGTNVQ LFVVGDQLLK GAALNAVQIA ELL //