ID G0WJI4_SOYBN Unreviewed; 376 AA.
AC G0WJI4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 08-NOV-2023, entry version 38.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:ADL27919.1};
RN [1] {ECO:0000313|EMBL:ADL27919.1}
RP NUCLEOTIDE SEQUENCE.
RA Jiang W., Liu C., Hu G., Chen Q.;
RL Submitted (MAR-2010) 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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00005076}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005021}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097}.
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; HM015631; ADL27919.1; -; mRNA.
DR AlphaFoldDB; G0WJI4; -.
DR OrthoDB; 1021986at2759; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR ExpressionAtlas; G0WJI4; baseline and differential.
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:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 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 2: Evidence at transcript level;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 41..156
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 171
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 284
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 376 AA; 41142 MW; D3C8ED7E286B643F CRC64;
MASLSVLRHN HLFSGPLPAR PKPTSSSSSR IRMSLRENGP SIAVVGVTGA VGQEFLSVLS
DRDFPYRSIH MLASKRSAGR RITFEDRDYV VQELTPESFD GVDIALFSAG GSISKHFGPI
AVNRGTVVVD NSSAFRMDEK VPLVIPEVNP EAMQNIKAGT GKGALIANPN CSTIICLMAA
TPLHRRAKVL RMVVSTYQAA SGAGAAAMEE LELQTREVLE GKPPTCKIFN RQYAFNLFSH
NASVLSNGYN EEEMKMVKET RKIWNDKDVK VTATCIRVPI MRAHAESVNL QFERPLDEDT
ARDILKNAPG VVVIDDRESN HFPTPLEVSN KDDVAVGRIR QDLSQDGNQG LDIFVCGDQI
RKGAALNAIQ IAEMLL
//
