ID   DHOM_MYCLE              Reviewed;         441 AA.
AC   P46806;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom; OrderedLocusNames=ML1129;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 3/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U15186; AAA63101.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31510.1; -; Genomic_DNA.
DR   PIR; T09992; T09992.
DR   RefSeq; NP_301823.1; NC_002677.1.
DR   RefSeq; WP_010908147.1; NC_002677.1.
DR   AlphaFoldDB; P46806; -.
DR   SMR; P46806; -.
DR   STRING; 272631.ML1129; -.
DR   EnsemblBacteria; CAC31510; CAC31510; CAC31510.
DR   KEGG; mle:ML1129; -.
DR   PATRIC; fig|272631.5.peg.2051; -.
DR   Leproma; ML1129; -.
DR   eggNOG; COG0460; Bacteria.
DR   HOGENOM; CLU_009116_1_0_11; -.
DR   OMA; LMFYGPG; -.
DR   BRENDA; 1.1.1.3; 3504.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000000806; Chromosome.
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   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR016204; HDH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW   Reference proteome; Threonine biosynthesis.
FT   CHAIN           1..441
FT                   /note="Homoserine dehydrogenase"
FT                   /id="PRO_0000066701"
FT   DOMAIN          356..435
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        207
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         13..20
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  45606 MW;  41EEC1939A5FD0F8 CRC64;
     MFSDERTVGV AVLGLGNVGS EVVRIIEGSA DDLAARIGAP LMLRGIGVRR VAVDRGVPVD
     LLTDNIEELV SRADVDIVVE VMGPVELSRK AILSALEHGK SVVTANKALL AASTGELAQA
     AESAHVDLYF EAAVAGAIPV IRPLTQSLAG DTVLRVAGIV NGTTNYILSA MDSTGADYDS
     ALAGARALGY AEADPTADVE GHDAAAKAAI LASIAFHTRV TADDVYREGI TKITPADFVS
     ARALGCTIKL LFICERITAA DGQQRVSARV YPALVPMSHP LATVSGAFNA VVVEAEAAGR
     LMFYGQGAGG APTASAVTGD LVMAARNRVL GSRGPKESKY AQLPMETIGF ISTRYYVSMN
     VADKPGVLSG VAAEFAKREV SIAEVRQEGV VDDGGRRVGA RIVVVTHGAT DAALSETVDA
     LADLDVVQGV TSVLRLEGIS L