ID A0A2N1T2S3_9SPIR Unreviewed; 333 AA. AC A0A2N1T2S3; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 20-JUN-2018, entry version 3. 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=CVV45_08125 {ECO:0000313|EMBL:PKL33336.1}; OS Spirochaetae bacterium HGW-Spirochaetae-10. OC Bacteria; Spirochaetes. OX NCBI_TaxID=2013833 {ECO:0000313|EMBL:PKL33336.1}; RN [1] {ECO:0000313|EMBL:PKL33336.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGW-Spirochaetae-10 {ECO:0000313|EMBL:PKL33336.1}; RX PubMed=28350393; DOI=.1038/ismej.2017.39; RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., RA Anantharaman K., Probst A., Burstein D., Thomas B.C., Banfield J.F.; RT "Potential for microbial H2 and metal transformations associated with RT novel bacteria and archaea in deep terrestrial subsurface sediments."; RL ISME J. 11:1915-1929(2017). RN [2] {ECO:0000313|EMBL:PKL33336.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGW-Spirochaetae-10 {ECO:0000313|EMBL:PKL33336.1}; RA Han C.G.; RL Submitted (NOV-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: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. {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|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: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 UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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 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 4 119 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. FT NP_BIND 11 14 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 39 40 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 158 159 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 128 128 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 99 99 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 155 155 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 235 235 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //