ID   DHOM_HELPY              Reviewed;         421 AA.
AC   P56429;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom; OrderedLocusNames=HP_0822;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07869.1; -; Genomic_DNA.
DR   PIR; F64622; F64622.
DR   RefSeq; NP_207615.1; NC_000915.1.
DR   RefSeq; WP_000746824.1; NC_018939.1.
DR   AlphaFoldDB; P56429; -.
DR   SMR; P56429; -.
DR   DIP; DIP-3530N; -.
DR   IntAct; P56429; 3.
DR   MINT; P56429; -.
DR   STRING; 85962.C694_04210; -.
DR   PaxDb; P56429; -.
DR   EnsemblBacteria; AAD07869; AAD07869; HP_0822.
DR   KEGG; hpy:HP_0822; -.
DR   PATRIC; fig|85962.47.peg.876; -.
DR   eggNOG; COG0460; Bacteria.
DR   OMA; LMFYGPG; -.
DR   PhylomeDB; P56429; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; 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:0009088; P:threonine biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR016204; HDH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW   Reference proteome; Threonine biosynthesis.
FT   CHAIN           1..421
FT                   /note="Homoserine dehydrogenase"
FT                   /id="PRO_0000066694"
FT   DOMAIN          343..418
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         10..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  46168 MW;  1C10A8C37D2C975B CRC64;
     MKKRLNIGLV GLGCVGSAVA KILQENQEII KDRAGVGIGI KKAVVRDVKK HKGYPFEISN
     DLESLIEDEE IDIVVELMGG VEAPYLLAKK TLAKQKAFVT ANKAMLAYHR YELEQTAKNT
     PIGFEASVCG GIPIIKALKD GLSANHILSF KGILNGTSNY ILSQMFKNQA SFKDALKDAQ
     HLGYAELNPE FDIKGIDAAH KLLILASLAY GIDAKLEEIL IEGIEKIEPD DMEFAKEFGY
     SIKLLGIAKK HPDCIELRVH PSMIKNECML SKVDGVMNAI SVIGDKVGET LYYGAGAGGE
     PTASAVISDI IEIARKKSSL MLGFETPQKL PLKPKEEIQC AYYARLLVSD EKGVFSQISA
     ILAQNDISLN NVLQKEILHS NKAKILFSTH TTNEKSMLNA LKELENLQSV LDTPKMIRLE
     N