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Database: UniProt
Entry: A0A1Y6F3R3_9SPHN
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ID   A0A1Y6F3R3_9SPHN        Unreviewed;       436 AA.
AC   A0A1Y6F3R3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
GN   ORFNames=SAMN06297468_1441 {ECO:0000313|EMBL:SMQ69219.1};
OS   Altererythrobacter xiamenensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Altererythrobacter.
OX   NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ69219.1, ECO:0000313|Proteomes:UP000194420};
RN   [1] {ECO:0000313|Proteomes:UP000194420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001406};
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|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|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; FXWG01000002; SMQ69219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6F3R3; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000194420; Unassembled WGS sequence.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
DR   CDD; cd04881; ACT_HSDH-Hom; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000579};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194420};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN          356..436
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        207
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         10..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         107
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   436 AA;  45727 MW;  F29FAFAE83C6B644 CRC64;
     MDKPLRIAIA GLGTVGTGVI RLLETNRDLL TARAGREIEV TAVSARDRNR NRGVDLSRYA
     WEDDMTALAA REDVDLVVEL VGGSDGPALA LARASLGAGK HFVTANKAMI AHHGIALAKT
     AEAHEAALKF EAAVAGGIPV VKGLREGTSA NALERIYGIL NGTCNYILSK MEDTGADFGE
     ILAEAQAKGF AEADPTFDIQ GIDAAHKLAI LAAIGFGARI DFDAVRTTGI TQVKAADIAQ
     ADALGFVIRL IAMADTETGE DGRTRLLQRV RPCLVPKDHP LASVDGPTNA VVAEGNFSGR
     LLFQGAGAGD GPTASAVVAD IIDIAREEIG APFSIPVAGL EPMPPVEPGH RMERTYLRFT
     VTDRPGVLAE ITAAMRDAGV SIESLIQKGR ADDGGEVLVA MVTHEGPERC IKEALDLLDG
     SESLTDAPLV LPILRD
//
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