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   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   ORFNames=SPBC776.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   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 IDENTIFICATION BY
RP   MASS 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:
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; CU329671; CAA22876.1; -; Genomic_DNA.
DR   PIR; T40673; T40673.
DR   RefSeq; NP_596318.1; NM_001022240.2.
DR   AlphaFoldDB; O94671; -.
DR   SMR; O94671; -.
DR   BioGRID; 277663; 3.
DR   STRING; 4896.SPBC776.03.1; -.
DR   iPTMnet; O94671; -.
DR   MaxQB; O94671; -.
DR   PaxDb; O94671; -.
DR   PRIDE; O94671; -.
DR   EnsemblFungi; SPBC776.03.1; SPBC776.03.1:pep; SPBC776.03.
DR   GeneID; 2541148; -.
DR   KEGG; spo:SPBC776.03; -.
DR   PomBase; SPBC776.03; -.
DR   VEuPathDB; FungiDB:SPBC776.03; -.
DR   eggNOG; KOG0455; Eukaryota.
DR   HOGENOM; CLU_009116_0_1_1; -.
DR   InParanoid; O94671; -.
DR   OMA; FNEFSTT; -.
DR   PhylomeDB; O94671; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   PRO; PR:O94671; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; ISO:PomBase.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009067; P:aspartate family amino acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009090; P:homoserine biosynthetic process; ISO:PomBase.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; ISO:PomBase.
DR   GO; GO:0009088; P:threonine biosynthetic process; ISO:PomBase.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR022697; HDH_short.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43070; PTHR43070; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF036497; HDH_short; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Threonine biosynthesis.
FT   CHAIN           1..376
FT                   /note="Probable homoserine dehydrogenase"
FT                   /id="PRO_0000066706"
FT   ACT_SITE        231
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         99
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
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