ID C5QSC8_9STAP Unreviewed; 329 AA. AC C5QSC8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 24-JUN-2015, entry version 33. 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:EES40262.1}; GN ORFNames=HMPREF0793_2134 {ECO:0000313|EMBL:EES40262.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES40262.1}; RN [1] {ECO:0000313|EMBL:EES40262.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES40262.1}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) 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|RuleBase:RU004041}. 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:EES40262.1}. 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; ACJB01000061; EES40262.1; -; Genomic_DNA. DR RefSeq; WP_002442811.1; NZ_GG696773.1. DR STRING; 525378.HMPREF0793_2134; -. DR EnsemblBacteria; EES40262; EES40262; HMPREF0793_2134. DR PATRIC; 31396054; VBIStaEpi14170_0592. 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-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 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 ECO:0000313|EMBL:EES40262.1}; KW Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 10 13 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 38 39 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 156 157 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 126 126 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121, FT ECO:0000256|PIRSR:PIRSR000148-1}. FT ACT_SITE 233 233 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 153 153 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 226 226 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 306 306 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 329 AA; 36471 MW; 613003F4A58917F4 CRC64; MTRLAVAGAT GLVGTKMLET LDRKNIPFDE LVLFSSARSA GKKVEFQGQT YTVQELTDEA ASEHFDYVLM SAGGGTSEHF APLFEQAGAI VIDNSSQWRM TEDVDLVVPE VNEPKFTRGI IANPNCSTIQ SVVPLKILKD AYGLKRVAYT TYQAVSGSGI KGKRDLSEGA NGKEPEAYPH PIYNNVLPHI DVFLENGYTK EEQKMIDETR KILNDKDLKV TATCVRVPVQ DSHSIEIDVT LDKDATVKDI QRLFEQDDRV VLVDNPEKNE YPLAIHSTGK DEVFVGRIRR DDSLDNTFHV WCTSDNLLKG AALNAVQVLE QVLTLKGAR //