ID   DHOM_BACSU              Reviewed;         433 AA.
AC   P19582; O32122; P70991;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   04-NOV-2008, entry version 66.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom; Synonyms=tdm; OrderedLocusNames=BSU32260;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=89008330; PubMed=3139660;
RA   Parsot C., Cohen G.N.;
RT   "Cloning and nucleotide sequence of the Bacillus subtilis hom gene
RT   coding for homoserine dehydrogenase. Structural and evolutionary
RT   relationships with Escherichia coli aspartokinases-homoserine
RT   dehydrogenases I and II.";
RL   J. Biol. Chem. 263:14654-14660(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-433.
RC   STRAIN=168;
RX   MEDLINE=87080286; PubMed=3098560;
RA   Parsot C.;
RT   "Evolution of biosynthetic pathways: a common ancestor for threonine
RT   synthase, threonine dehydratase and D-serine dehydratase.";
RL   EMBO J. 5:3013-3019(1986).
CC   -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4-
CC       semialdehyde + NAD(P)H.
CC   -!- ENZYME REGULATION: Feedback inhibition by threonine.
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; M23217; AAA50609.1; -; Genomic_DNA.
DR   EMBL; Z99120; CAB15216.1; -; Genomic_DNA.
DR   EMBL; X04603; CAA28269.1; -; Genomic_DNA.
DR   PIR; A31973; DEECHS.
DR   RefSeq; NP_391106.1; -.
DR   GeneID; 936654; -.
DR   GenomeReviews; AL009126_GR; BSU32260.
DR   KEGG; bsu:BSU32260; -.
DR   NMPDR; fig|224308.1.peg.3232; -.
DR   SubtiList; BG10460; hom.
DR   HOGENOM; P19582; -.
DR   BioCyc; BSUB224308:BSU3223-MON; -.
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    433       Homoserine dehydrogenase.
FT                                /FTId=PRO_0000066692.
FT   DOMAIN      349    424       ACT.
FT   NP_BIND       9     16       NADP (By similarity).
FT   ACT_SITE    205    205       Proton donor (Potential).
FT   BINDING     105    105       NADP (By similarity).
FT   BINDING     190    190       Substrate (By similarity).
FT   CONFLICT    375    375       S -> T (in Ref. 3; CAA28269).
FT   CONFLICT    402    402       E -> Q (in Ref. 1; AAA50609).
SQ   SEQUENCE   433 AA;  47494 MW;  03E9DF7727D62696 CRC64;
     MKAIRVGLLG LGTVGSGVVK IIQDHQDKLM HQVGCPVTIK KVLVKDLEKK REVDLPKEVL
     TTEVYDVIDD PDVDVVIEVI GGVEQTKQYL VDALRSKKHV VTANKDLMAV YGSELLAEAK
     ENGCDIYFEA SVAGGIPILR TLEEGLSSDR ITKMMGIVNG TTNFILTKMI KEKSPYEEVL
     KEAQDLGFAE ADPTSDVEGL DAARKMAILA RLGFSMNVDL EDVKVKGISQ ITDEDISFSK
     RLGYTMKLIG IAQRDGSKIE VSVQPTLLPD HHPLSAVHNE FNAVYVYGEA VGETMFYGPG
     AGSMPTATSV VSDLVAVMKN MRLGVTGNSF VGPQYEKNMK SPSDIYAQQF LRIHVKDEVG
     SFSKITSVFS ERGVSFEKIL QLPIKGHDEL AEIVIVTHHT SEADFSDILQ NLNDLEVVQE
     VKSTYRVEGN GWS
//