ID B6AT19_9RHOB Unreviewed; 417 AA.
AC B6AT19;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN Name=hom {ECO:0000313|EMBL:EDZ42608.1};
GN ORFNames=RB2083_2123 {ECO:0000313|EMBL:EDZ42608.1};
OS Rhodobacteraceae bacterium HTCC2083.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ42608.1, ECO:0000313|Proteomes:UP000005746};
RN [1] {ECO:0000313|Proteomes:UP000005746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX PubMed=21036993; DOI=10.1128/JB.01268-10;
RA Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT Roseobacter.";
RL J. Bacteriol. 193:319-320(2011).
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; DS995276; EDZ42608.1; -; Genomic_DNA.
DR AlphaFoldDB; B6AT19; -.
DR STRING; 314270.RB2083_2123; -.
DR eggNOG; COG0460; Bacteria.
DR HOGENOM; CLU_009116_1_0_5; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000005746; 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: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 NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EDZ42608.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005746}.
FT DOMAIN 339..415
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 96
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 417 AA; 43738 MW; F51C5BDA8E6A7E82 CRC64;
MGTVGTGVVK IIRQQAALLS ARAGRDVVIS AVSARDQSRD RGVSLSGYAW ETDAVALAKR
DDVDVFVELI GGDTGVAKAA VEAALALGKD VVTANKALLA HHGQALAQMA EANDSIIRYE
AAVAGGIPVI KSLLEGLAGN EITRVMGVMN GTCNYILTNM EKSGRGYNAL FDECAELGYL
EADPNLDVGG IDASHKLALL ASIAFGTQVD FDAVELEGIQ RIELQDINHA ADMGFRIKLL
GVTQMTGRGL EQRMTPCLVP SASPLGQLEG GTNMVVIEGN HVEQIVLRGP GAGMGPTASA
VMGDVMDIAR GIRIPTFGIP ADQLQKATSA KAASPAPFYL RVGLKDKPGA MAKIATILGE
AGISIDRMRQ LGHADETAPV LIVTHKCMRQ TLDEALTQIG KSEVVATRPV ALRIENL
//
