(data stored in ACNUC6288 zone)

SWISSPROT: Q6BN01_DEBHA

ID   Q6BN01_DEBHA            Unreviewed;       360 AA.
AC   Q6BN01;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|RuleBase:RU000579};
DE            Short=HDH {ECO:0000256|PIRNR:PIRNR036497};
DE            EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|RuleBase:RU000579};
GN   OrderedLocusNames=DEHA2F01298g {ECO:0000313|EMBL:CAG88723.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 /
OS   IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88723.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88723.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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         Evidence={ECO:0000256|PIRNR:PIRNR036497,
CC         ECO:0000256|RuleBase:RU000579};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5. {ECO:0000256|RuleBase:RU000579}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; CR382138; CAG88723.1; -; Genomic_DNA.
DR   RefSeq; XP_460419.1; XM_460419.1.
DR   STRING; 4959.XP_460419.1; -.
DR   EnsemblFungi; CAG88723; CAG88723; DEHA2F01298g.
DR   GeneID; 2903819; -.
DR   KEGG; dha:DEHA2F01298g; -.
DR   HOGENOM; HOG000024037; -.
DR   InParanoid; Q6BN01; -.
DR   KO; K00003; -.
DR   OMA; WSEVVAQ; -.
DR   OrthoDB; 998704at2759; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009090; P:homoserine biosynthetic process; IEA:EnsemblFungi.
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:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR022697; HDH_short.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   3: Inferred from homology;
DR   PRODOM; Q6BN01.
DR   SWISS-2DPAGE; Q6BN01.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Isoleucine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|PIRSR:PIRSR036497-2,
KW   ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN          11..132
FT                   /note="NAD_binding_3"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          149..352
FT                   /note="Homoserine_dh"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   NP_BIND         11..16
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT   BINDING         89
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         113
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         207
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ   SEQUENCE   360 AA;  38789 MW;  2B28967D21A9998A CRC64;
     MVKSVNVAII GSGVVGSAFV NQLKNLKTAI NFNVVYFARS SKEALFSSDY KPVDLASYKN
     ASAQAVLSLD ELTKFLKGAS KPTILIDNTS NSTIADYYPT FVKEGISIAT PNKKAFSSDL
     SVWNEIFKNS EAPSGGLVYH EATVGAGLPI IGPLRDLITT GDKVEKIEGI FSGTLSYIFN
     EFSTTDPSTK VKFSDVVKVA KDLGYTEPDP RDDLNGLDVA RKVTILARIS GFDVESPTSF
     PVESLIPKEL ESVQTADEFL SKLPDFDADI QKVKEEALAE NKVLRFVGQV DFKANKVSVE
     IGKYGFDHPF ASLKGSDNVV SIKTERYSNP LIIQGAGAGA EVTAHGVLAD AIKIAERIAI
//

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