ID D3PLR0_MEIRD Unreviewed; 338 AA.
AC D3PLR0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN OrderedLocusNames=Mrub_2400 {ECO:0000313|EMBL:ADD29151.1};
GN ORFNames=K649_10530 {ECO:0000313|EMBL:AGK05398.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK05398.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:ADD29151.1, ECO:0000313|Proteomes:UP000006655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC {ECO:0000313|EMBL:ADD29151.1};
RX PubMed=21304689; DOI=10.4056/sigs.1032748;
RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Meiothermus ruber type strain (21).";
RL Stand. Genomic Sci. 3:26-36(2010).
RN [2] {ECO:0000313|EMBL:AGK05398.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK05398.1};
RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA Eichler E., Turner S.W.;
RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT Sequencing Data.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGK05398.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC {ECO:0000313|EMBL:AGK05398.1};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001743; ADD29151.1; -; Genomic_DNA.
DR EMBL; CP005385; AGK05398.1; -; Genomic_DNA.
DR RefSeq; WP_013014649.1; NC_021081.1.
DR AlphaFoldDB; D3PLR0; -.
DR STRING; 504728.K649_10530; -.
DR KEGG; mrb:Mrub_2400; -.
DR KEGG; mre:K649_10530; -.
DR PATRIC; fig|504728.9.peg.2170; -.
DR eggNOG; COG0460; Bacteria.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000006655; Chromosome.
DR Proteomes; UP000013026; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR022697; HDH_short.
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 PIRSF; PIRSF036497; HDH_short; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|PIRSR:PIRSR036497-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADD29151.1}.
FT DOMAIN 10..121
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 131..308
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 101
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ SEQUENCE 338 AA; 36011 MW; B78BED994D327C3D CRC64;
METVRVALMG GGTVGSAFAQ LLPAHQARFS ALGVKVELAR VLVRDIEKSR PGIPSRLLTN
NPKGFLDDVD VLVEVAGGTT TAGDLVLQAL EMGLPVVTAN KALLAERWDE LREYAEQGDL
HYEASVMAGT PIIGALQSLW GNQTLEMHGI VNGTCSYLIR RMEEGASYEQ AFKEAGDLGY
LEADPNLDVG GIDSAHKICV LGRLTVDPGL SWEKVLRRTR GIQHLTPELL RQARAEGYAI
KLVASLYPEN GEWVAAVRPV RLPASHPLVT MGSGRNAMVY RGEPVGQLVF AGAGAGGGVT
ASAVLGDLYR VLLGTPGHLP IPSATPLPQQ AVEQLEEV
//
