DHAS_PROMA
ID DHAS_PROMA Reviewed; 343 AA.
AC P49420;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
DE Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
DE Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121};
DE EC=1.2.1.11 {ECO:0000255|HAMAP-Rule:MF_02121};
DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; OrderedLocusNames=Pro_1814;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 238-343.
RC STRAIN=SARG / CCMP1375 / SS120;
RA Lorenz M., Boerner T., Hess W.R.;
RT "Molecular cloning and characterization of a dihydrodipicolinate synthase
RT (DHDPS) gene from the photoautotrophic prokaryote Prochlorococcus marinus
RT CCMP 1375 (Prochlorophyta).";
RL Endocyt. Cell Res. 11:59-68(1995).
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:0000255|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:0000255|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:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_02121}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000255|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; AE017126; AAQ00858.1; -; Genomic_DNA.
DR EMBL; Z68126; CAA92210.1; -; Genomic_DNA.
DR RefSeq; NP_876205.1; NC_005042.1.
DR RefSeq; WP_011125963.1; NC_005042.1.
DR AlphaFoldDB; P49420; -.
DR SMR; P49420; -.
DR STRING; 167539.Pro_1814; -.
DR PRIDE; P49420; -.
DR EnsemblBacteria; AAQ00858; AAQ00858; Pro_1814.
DR GeneID; 54201144; -.
DR KEGG; pma:Pro_1814; -.
DR PATRIC; fig|167539.5.peg.1916; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_0_1_3; -.
DR OMA; CEEEMKM; -.
DR OrthoDB; 1799040at2; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000001420; 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; Diaminopimelate biosynthesis; Lysine biosynthesis;
KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..343
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141386"
FT ACT_SITE 137
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 20..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 48..49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 108
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 167..168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 221
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 323
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT CONFLICT 238
FT /note="T -> P (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..246
FT /note="VPV -> GPA (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..254
FT /note="SI -> AT (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..260
FT /note="EFAE -> VFSG (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..270
FT /note="KI -> QN (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="N -> D (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="K -> Q (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="I -> K (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="I -> K (in Ref. 2; CAA92210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 37557 MW; E20036130DB7403B CRC64;
MTLQKPFPDR PLTLAVLGSS GAVGAEILKI LEERSFPIRE LRLLASERSA GQVQFFKGED
LVVKKVSPEG FEDVDLVLAS AGGSISRKWR KVINSAGAVI VDNSNAYRME PDVPLVVPEV
NPSQVFTHKG LIANPNCTTI LLALVLAPLS AQLPIKRVVV STYQSASGAG ARAMNELKQL
SQDVLNGNIP KSEILPYSLA FNLFLHNSPL QSNNYCEEEM KMINETRKIL NQSELAITAT
CVRVPVLRAH SESINIEFAE PFPVEEARKI LSNASGIKLL EDIQMNRFPM PIDVTGKDDI
AVGRIRQDLS NPKALELWLC GDQIRKGAAL NAIQIAELLL TRS
