ID J9Z2Q5_9PROT Unreviewed; 430 AA.
AC J9Z2Q5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=HIMB59_00013950 {ECO:0000313|EMBL:AFS49570.1};
OS alpha proteobacterium HIMB59.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=744985 {ECO:0000313|EMBL:AFS49570.1, ECO:0000313|Proteomes:UP000006097};
RN [1] {ECO:0000313|EMBL:AFS49570.1, ECO:0000313|Proteomes:UP000006097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB59 {ECO:0000313|EMBL:AFS49570.1,
RC ECO:0000313|Proteomes:UP000006097};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (AUG-2012) 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 -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006753}.
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DR EMBL; CP003801; AFS49570.1; -; Genomic_DNA.
DR AlphaFoldDB; J9Z2Q5; -.
DR STRING; 744985.HIMB59_00013950; -.
DR KEGG; apc:HIMB59_00013950; -.
DR eggNOG; COG0460; Bacteria.
DR HOGENOM; CLU_009116_1_0_5; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000006097; Chromosome.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; 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; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AFS49570.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006097}.
FT DOMAIN 349..430
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 430 AA; 47798 MW; 6BA91CA4449A8398 CRC64;
MNKIKIAIFG LGVVGSHVVK LLEKNNNILN GSKFEIVALG AKNKSKKRNF NVKKYNWVSH
FSDLENYAKP DVIIETIGGT GSYINNLYKY CIKKNISLIT ANKAQLAENG DKFFADFDNQ
KLFLGFEAAV LGAVPVVRSI EQSILPSKVN KIYGIFNGTT NYIISQMYDN KISFQESLNQ
AIKNGFAEQD SSADLSGRDA NHKLVLLSNL SFGNKFSFSD INYDGIENIK LIDLEQGLKL
GYKLKLVSLT ERYSNSKFYS SVAPCFVPEN SLIAKTDFEE NVITLEGDSF IKTSLVGKGA
GGYPTATSII SDLKRFISHD ETNGVFVKKY SSMPKSKFVN RSDRKRPYYL RMSVSNKVGV
LKSIAQIFSQ KSISIKSIIQ LNTSNEKTVP IVIISDPAGV DKINSVTQNL KKTSFIKKEI
SVIRIEENIG
//
