ID A0A1Q5T105_9EURO Unreviewed; 380 AA.
AC A0A1Q5T105;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=PENSUB_12218 {ECO:0000313|EMBL:OKO93939.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO93939.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO93939.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO93939.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKO93939.1}.
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DR EMBL; MNBE01000723; OKO93939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5T105; -.
DR STRING; 1316194.A0A1Q5T105; -.
DR OrthoDB; 2208447at2759; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000186955; 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: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; 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 SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955}.
FT DOMAIN 23..157
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 166..373
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
SQ SEQUENCE 380 AA; 40291 MW; 65F66719B1B7F8E2 CRC64;
MKQQAFLTRC LMVQGSIQVH HYGVGGVGNA FLEQLGQLSN PPKLVLLARS TQTLMSAAPT
YSPCIPFTTW EDAAKSPSLA KSNALPPAEI AAFLASAPGR AIVVDNTSDL TLAQAYPIFL
ERGVSVVTPN KKGFSEDITL FNDIFSSAVR GNALVYHQCT VGGTLPVLST LRDLVSTGDA
IIRVEGVLSG TLSLLLGEFM PGNGTSSAQW SFLVSHAKEI GHTEPDPRDD LNGLDFARKL
TIIARVIGVE VTSPDSFPVE SLIPVELSTI PSSAEGIAQF MSELPKFDAH MDAAKNSAEK
QGKILRYIGS IDVTTGAIEV GLRHVEKGSP IANLQGSQIV SIYTKRYGTN PLILQGGGGG
GEITAMGLMA DLLKAMERLK
//
