ID   DHOM_MYCTU              Reviewed;         441 AA.
AC   P63629; Q10601;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   04-NOV-2008, entry version 26.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom; Synonyms=thrA; OrderedLocusNames=Rv1294, MT1333;
GN   ORFNames=MTCY373.14;
OS   Mycobacterium tuberculosis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   MEDLINE=22206494; PubMed=12218036;
RX   DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; BX842576; CAA97759.1; -; Genomic_DNA.
DR   EMBL; AE000516; AAK45595.1; -; Genomic_DNA.
DR   PIR; B70773; B70773.
DR   RefSeq; NP_215810.1; -.
DR   RefSeq; NP_335781.1; -.
DR   GeneID; 886962; -.
DR   GeneID; 924737; -.
DR   GenomeReviews; AE000516_GR; MT1333.
DR   GenomeReviews; AL123456_GR; Rv1294.
DR   KEGG; mtc:MT1333; -.
DR   KEGG; mtu:Rv1294; -.
DR   TIGR; MT1333; -.
DR   TubercuList; Rv1294; -.
DR   HOGENOM; P63629; -.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
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_0000066702.
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;  45553 MW;  818248C137885BE8 CRC64;
     MPGDEKPVGV AVLGLGNVGS EVVRIIENSA EDLAARVGAP LVLRGIGVRR VTTDRGVPIE
     LLTDDIEELV AREDVDIVVE VMGPVEPSRK AILGALERGK SVVTANKALL ATSTGELAQA
     AESAHVDLYF EAAVAGAIPV IRPLTQSLAG DTVLRVAGIV NGTTNYILSA MDSTGADYAS
     ALADASALGY AEADPTADVE GYDAAAKAAI LASIAFHTRV TADDVYREGI TKVTPADFGS
     AHALGCTIKL LSICERITTD EGSQRVSARV YPALVPLSHP LAAVNGAFNA VVVEAEAAGR
     LMFYGQGAGG APTASAVTGD LVMAARNRVL GSRGPRESKY AQLPVAPMGF IETRYYVSMN
     VADKPGVLSA VAAEFAKREV SIAEVRQEGV VDEGGRRVGA RIVVVTHLAT DAALSETVDA
     LDDLDVVQGV SSVIRLEGTG L
//