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Database: UniProt
Entry: A0A1G6TW60_9ACTN
LinkDB: A0A1G6TW60_9ACTN
Original site: A0A1G6TW60_9ACTN 
ID   A0A1G6TW60_9ACTN        Unreviewed;       425 AA.
AC   A0A1G6TW60;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013376};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=SAMN05216270_103182 {ECO:0000313|EMBL:SDD33144.1};
OS   Glycomyces harbinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=58114 {ECO:0000313|EMBL:SDD33144.1, ECO:0000313|Proteomes:UP000198949};
RN   [1] {ECO:0000313|EMBL:SDD33144.1, ECO:0000313|Proteomes:UP000198949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDD33144.1,
RC   ECO:0000313|Proteomes:UP000198949};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|ARBA:ARBA00000116};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005062}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006753}.
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DR   EMBL; FNAD01000003; SDD33144.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6TW60; -.
DR   STRING; 58114.SAMN05216270_103182; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000198949; 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: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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          348..421
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         6..13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         103
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   425 AA;  44423 MW;  E3A147054DB71F00 CRC64;
     MKLALLGCGT VGSEVVRLMR TRGEELAARV GEPVEIVGIA VRRIDRDRSH LPVDESLFTT
     DALGLVKRDD VDIVVEVAGG IEPARTWILT ALGQGKSVVT ANKALLAEDG PALAAAAKDG
     GADLYYEASA AAAIPLMRPL RESLHGDKIN RVLGIVNGTT NFICTAMSTK GTSFEEALAE
     ATDLGYAEAD PTADVDNYDA AAKAALIASL AFHTHVDLKD VYREPLRGIS ATDIASAAAE
     GRVVKPLCIA TREADGVSVR VHPAMIPATH PLANVNGAYN AVFVEAESAG RLMFYGAGAG
     GTETASAVLG DIVAVARNKR GGITAFPPEA AYSDLPVKPI GEARTRYHVS LDVVDEPGVL
     ARVAATFAHH GVSLATVHQS GRGDDAQLVV VTHTAADKQL SDTVKELTQL TSVHQVTSVM
     RVEGE
//
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