ID M9R7A2_9RHOB Unreviewed; 340 AA. AC M9R7A2; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 18-JAN-2017, entry version 23. 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:AGI66211.1}; GN ORFNames=OAN307_c04730 {ECO:0000313|EMBL:AGI66211.1}; OS Octadecabacter antarcticus 307. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Octadecabacter. OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI66211.1, ECO:0000313|Proteomes:UP000005307}; RN [1] {ECO:0000313|EMBL:AGI66211.1, ECO:0000313|Proteomes:UP000005307} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=307 {ECO:0000313|EMBL:AGI66211.1}; RX PubMed=23671678; RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K., RA Brinkhoff T., Simon M., Daniel R.; RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High RT Genome Plasticity and a New Type of Xanthorhodopsin."; RL PLoS ONE 8:E63422-E63422(2013). 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|RuleBase:RU004041, ECO:0000256|SAAS:SAAS00558004}. 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; CP003740; AGI66211.1; -; Genomic_DNA. DR RefSeq; WP_015498260.1; NC_020911.1. DR STRING; 391626.OA307_4917; -. DR EnsemblBacteria; AGI66211; AGI66211; OAN307_c04730. DR KEGG; oat:OAN307_c04730; -. DR eggNOG; ENOG4105CM3; Bacteria. DR eggNOG; COG0136; LUCA. DR KO; K00133; -. DR OrthoDB; POG091H00EF; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000005307; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR016040; NAD(P)-bd_dom. 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 PIRSF; PIRSF000148; ASA_dh; 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:UP000005307}; 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 ECO:0000313|EMBL:AGI66211.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005307}; 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 160 161 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 130 130 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121, FT ECO:0000256|PIRSR:PIRSR000148-1}. FT ACT_SITE 243 243 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121, ECO:0000256|PIRSR:PIRSR000148- FT 1}. FT BINDING 99 99 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 157 157 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 236 236 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 316 316 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 340 AA; 37452 MW; 5DAD37143A1CA978 CRC64; MGYRIVIAGA TGNVGREMLN ILAERQFPVD EVVVLASRRS LGTEVSFGDR TLKTLDLDTF DFTGYDIAFF AVGSDATKKY APIAAKQGCV VIDNSSLYRY DPDVPLVVPE VNPEAVDGYA KKNIIANPNC STAQMVVALK PLHDRAKIKR VVVSTYQSVS GSGKDAIDEL WDQTKSIYNP TDSKPPKVFT KQIAFNVIPH IDVFMDSGDT KEEWKMVAET KKIIDKSIKV TATCVRVPVF VGHSESINIE FEDFIDEDEA RDILREAPGV MVIDKREDGG YVTPVECVGD FATFVSRIRQ DSTIDNGLNM WVVSDNLRKG AALNAVQIAE TLGNRCLKKG //