ID E3RR65_PYRTT Unreviewed; 371 AA.
AC E3RR65;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 08-NOV-2023, entry version 50.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|PIRNR:PIRNR036497};
DE Short=HDH {ECO:0000256|PIRNR:PIRNR036497};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|PIRNR:PIRNR036497};
GN ORFNames=PTT_11276 {ECO:0000313|EMBL:EFQ91798.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ91798.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ91798.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|PIRNR:PIRNR036497};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036497}.
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DR EMBL; GL534607; EFQ91798.1; -; Genomic_DNA.
DR RefSeq; XP_003300120.1; XM_003300072.1.
DR AlphaFoldDB; E3RR65; -.
DR STRING; 861557.E3RR65; -.
DR EnsemblFungi; EFQ91798; EFQ91798; PTT_11276.
DR KEGG; pte:PTT_11276; -.
DR eggNOG; KOG0455; Eukaryota.
DR HOGENOM; CLU_009116_0_1_1; -.
DR OrthoDB; 5487989at2759; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
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 InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR022697; HDH_short.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43070; -; 1.
DR PANTHER; PTHR43070:SF5; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF036497; HDH_short; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR036497};
KW Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW Isoleucine biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW NADP {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|PIRSR:PIRSR036497-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036497};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR036497}.
FT DOMAIN 13..143
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 161..364
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 233
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT BINDING 13..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ SEQUENCE 371 AA; 39937 MW; 9F93AABD4F0FBC73 CRC64;
MPLPRQVFIA VIGAGGVGKA FLSQLSTLSK RLSQSPSSPY YLSLIWLSTS KKAVYHSDYK
SLSNWESELE NASKPALPLP QLCEYLQKAP GKVVLVDNTS SQDVADSYPD FLKKGISIVT
PNKKAFSGSY DLWSRIFDAA ANGNGAGGYV FHESSVGAGL PIISTLKDLV ETGDEITKIE
GVFSGTMSFL FNSFQPLGGG GGKFSAEVKN AKEKGYTEPD ARDDLNGLDV ARKLTILARL
SGLKVESPTS FPVDSLIPKE LESCSSGDEF LEKLPQYDDR MEKLKAEAAQ EGKVIRFVGS
LKVPSNEVKV GLEKFDQNHA IAQLKGSDNI IAFYTKRYGD NPLIVQGAGA GGDVTAMGVT
ADLIKVLRLL H
//
