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   22-JUL-2008, entry version 54.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom; OrderedLocusNames=ML1129;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
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   MEDLINE=21128732; 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: L-homoserine + NAD(P)(+) = L-aspartate 4-
CC       semialdehyde + NAD(P)H.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 ACT domain.
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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; -.
DR   GeneID; 910223; -.
DR   GenomeReviews; AL450380_GR; ML1129.
DR   KEGG; mle:ML1129; -.
DR   NMPDR; fig|272631.1.peg.695; -.
DR   Leproma; ML1129; -.
DR   HOGENOM; P46806; -.
DR   BioCyc; MLEP272631:ML1129-MON; -.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR005106; Asp/hSer_DHase_NAD-bd.
DR   InterPro; IPR016204; hSer_DHase.
DR   InterPro; IPR001342; hSer_DHase_cat.
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   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Isoleucine biosynthesis; Methionine biosynthesis;
KW   NADP; Oxidoreductase; Threonine biosynthesis.
FT   CHAIN         1    441       Homoserine dehydrogenase.
FT                                /FTId=PRO_0000066701.
FT   DOMAIN      355    433       ACT.
FT   NP_BIND      13     20       NADP (By similarity).
FT   ACT_SITE    207    207       Proton donor (Potential).
FT   BINDING     107    107       NADP (By similarity).
FT   BINDING     192    192       Substrate (By similarity).
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
//