ID K9YA92_HALP7 Unreviewed; 431 AA.
AC K9YA92;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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};
DE Flags: Precursor;
GN OrderedLocusNames=PCC7418_1573 {ECO:0000313|EMBL:AFZ43759.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ43759.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003945; AFZ43759.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YA92; -.
DR STRING; 65093.PCC7418_1573; -.
DR KEGG; hao:PCC7418_1573; -.
DR PATRIC; fig|65093.3.peg.1676; -.
DR eggNOG; COG0460; Bacteria.
DR HOGENOM; CLU_009116_1_0_3; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000010481; Chromosome.
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:UP000010481};
KW Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 351..431
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 204
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 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 431 AA; 45813 MW; 790A25F6C481A6F6 CRC64;
MVESLKIGLL GLGTVGTATA SILLSPESRH PLLKSIEIAK VGVKTVDKRR GVDFPEGVLT
TDLEGIISDP EIDIVVELMG GLEPARSLIL KAITNGKHIV TANKAVISRY GEEIYRAADT
KGVYVLIEAA VGGGIPVIRP LQQALSVNQI QSILGIINGT TNFILTKMTA EGSDFADVLT
EAQELGYAEA DPSADVDGYD AADKITILAT LAFGQQVNLD QVSCEGIRQV SAVDIQYAKQ
LGFEIKLLAI AQQEEKGLQV RVHPTLVPKS HPLASIDGVN NAVLLEGDPI GQVMFYGPGA
GGGATASAVV SDVLNIAAML TTNGSVNPLM KIPQHPSSEL VSIAELVTRF YARIICVDRP
GVIGNLGTCF GKNDVSLESI VQIDFQNGMA EIVVVTHNVK EENFRQALAQ IPQLEAIDQI
EIPSVLRVLR E
//
