ID   DHOM_SCHPO              Reviewed;         376 AA.
AC   O94671;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Probable homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   ORFNames=SPBC776.03;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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.
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DR   EMBL; CU329671; CAA22876.1; -; Genomic_DNA.
DR   PIR; T40673; T40673.
DR   RefSeq; NP_596318.1; -.
DR   HSSP; P31116; 1EBF.
DR   GeneID; 2541148; -.
DR   KEGG; spo:SPBC776.03; -.
DR   NMPDR; fig|4896.1.peg.2184; -.
DR   GeneDB_Spombe; SPBC776.03; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004336-MON; -.
DR   ArrayExpress; O94671; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005106; Asp/hSer_DHase_NAD-bd.
DR   InterPro; IPR001342; hSer_DHase_cat.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Isoleucine biosynthesis; Methionine biosynthesis;
KW   NADP; Oxidoreductase; Phosphoprotein; Threonine biosynthesis.
FT   CHAIN         1    376       Probable homoserine dehydrogenase.
FT                                /FTId=PRO_0000066706.
FT   NP_BIND      13     20       NADP (By similarity).
FT   ACT_SITE    231    231       Proton donor (Potential).
FT   BINDING      99     99       NADP (By similarity).
FT   BINDING     123    123       NADP (By similarity).
FT   BINDING     216    216       Substrate (By similarity).
FT   MOD_RES     201    201       Phosphoserine.
SQ   SEQUENCE   376 AA;  40037 MW;  3A2BC3A2CBA9263C CRC64;
     MSASRTNVNV AIVGTGNIGG ELLNQIKGFN ENASTNGTTS FNVVAISSME GHYVSKDYQP
     INLSEWKNLT SQNQGAYSLD ALVDFLAKSP LPAILVDNTA SEAIAQSYPK FLSKKINIAT
     PNKKAFSASN DVYQNIIKAS KESGALLMHE ASVGAGLPII STLKELIATG DEIIKIEGIF
     SGTLSYIFNV WSPNGKKGTA SFSDIVKIAK QNGYTEPDPR DDLNGMDVAR KVTILSRIAG
     VHVESASSFP VKSLIPEPLK SAVNAEEFLA GLPNFDSEFA SMREEAEKEG KVVRFVGEAD
     VANKTTLVKL EKYDASHPFA NLQSSDNIIS FTTKRYHTRP LVVIGAGAGA AVTAAGVLGD
     MIKIMSQVRA SDAPSA
//