ID A0A1H9CMY5_9ACTN Unreviewed; 364 AA.
AC A0A1H9CMY5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN ORFNames=SAMN05216481_103333 {ECO:0000313|EMBL:SEQ02570.1};
OS Streptomyces radiopugnans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=403935 {ECO:0000313|EMBL:SEQ02570.1, ECO:0000313|Proteomes:UP000199055};
RN [1] {ECO:0000313|EMBL:SEQ02570.1, ECO:0000313|Proteomes:UP000199055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3519 {ECO:0000313|EMBL:SEQ02570.1,
RC ECO:0000313|Proteomes:UP000199055};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; FOET01000003; SEQ02570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9CMY5; -.
DR STRING; 403935.SAMN05216481_103333; -.
DR Proteomes; UP000199055; Unassembled WGS sequence.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000199055}.
FT DOMAIN 19..134
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 144
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 364 AA; 37696 MW; 541404E29FAF0F41 CRC64;
MTPAGGFPRA PIGRADRPTL AVVGATGAAG TVLLGLLSER ADVWGEIRLV ASERSAGRKL
AVRGEEVEVL ALGEEVFDGV DVAMFDVPAE VAARWAPVAA ARGAVVVDNS GAFRTDPDVP
LVVPEVNAHA ARNRPRGIVA GPGCATLTMI VALGALHAEW ALEELVVSTY QAVSESGRRG
VEALRGQLAA VAGAELGVHP GDVRRAVGDT GPYAAPIALN VVPFSGTPAE DGWTTEELAV
REETRRVLGL PGLRATATCV RVPVVTTHSV SVHARFESEV SVGKAHEILA NAPGVVVCDD
PVAGEFPTPA DAVGTDPVWA GRVRRSPDDP RALELFVCGD NLRKGAALNM AQIGELVAAE
RAED
//
