DHOM_CORGL
ID DHOM_CORGL Reviewed; 445 AA.
AC P08499;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Homoserine dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.3;
GN Name=hom; Synonyms=thrA; OrderedLocusNames=Cgl1183, cg1337;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=2835591; DOI=10.1111/j.1365-2958.1988.tb00007.x;
RA Peoples O.P., Liebl W., Bodis M., Maeng P.J., Follettie M.T.,
RA Archer J.A.C., Sinskey A.J.;
RT "Nucleotide sequence and fine structural analysis of the Corynebacterium
RT glutamicum hom-thrB operon.";
RL Mol. Microbiol. 2:63-72(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3320973; DOI=10.1093/nar/15.24.10598;
RA Mateos L.M., del Real G., Aguilar A., Martin J.F.;
RT "Nucleotide sequence of the homoserine dehydrogenase (thr A) gene of
RT Brevibacterium lactofermentum.";
RL Nucleic Acids Res. 15:10598-10598(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9362124; DOI=10.1271/bbb.61.1760;
RA Sugimoto M., Tanaka A., Suzuki T., Matsui H., Nakamori S., Takagi H.;
RT "Sequence analysis of functional regions of homoserine dehydrogenase genes
RT from L-lysine and L-threonine-producing mutants of Brevibacterium
RT lactofermentum.";
RL Biosci. Biotechnol. Biochem. 61:1760-1762(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [6]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=4394351; DOI=10.1093/oxfordjournals.jbchem.a129361;
RA Miyajima R., Shiio I.;
RT "Regulation of aspartate family amino acid biosynthesis in Brevibacterium
RT flavum. 3. Properties of homoserine dehydrogenase.";
RL J. Biochem. 68:311-319(1970).
RN [7]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=1743520; DOI=10.1016/0378-1119(91)90296-n;
RA Archer J.A., Solow-Cordero D.E., Sinskey A.J.;
RT "A C-terminal deletion in Corynebacterium glutamicum homoserine
RT dehydrogenase abolishes allosteric inhibition by L-threonine.";
RL Gene 107:53-59(1991).
RN [8]
RP MUTANT RESISTANT TO FEEDBACK INHIBITION (FBR).
RX PubMed=1902466; DOI=10.1128/jb.173.10.3228-3230.1991;
RA Reinscheid D.J., Eikmanns B.J., Sahm H.;
RT "Analysis of a Corynebacterium glutamicum hom gene coding for a feedback-
RT resistant homoserine dehydrogenase.";
RL J. Bacteriol. 173:3228-3230(1991).
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:0000269|PubMed:1743520, ECO:0000269|PubMed:4394351};
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:0000269|PubMed:1743520, ECO:0000269|PubMed:4394351};
CC -!- ACTIVITY REGULATION: Feedback inhibition by threonine.
CC {ECO:0000269|PubMed:1743520, ECO:0000269|PubMed:4394351}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=190 uM for L-aspartate 4-semialdehyde
CC {ECO:0000269|PubMed:4394351};
CC KM=37.4 uM for NADPH {ECO:0000269|PubMed:4394351};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:4394351};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Y00546; CAA68614.1; -; Genomic_DNA.
DR EMBL; Y00476; CAA68536.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98576.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19887.1; -; Genomic_DNA.
DR PIR; S00865; DEFKHG.
DR RefSeq; NP_600409.1; NC_003450.3.
DR RefSeq; WP_003854900.1; NC_006958.1.
DR AlphaFoldDB; P08499; -.
DR SMR; P08499; -.
DR STRING; 196627.cg1337; -.
DR World-2DPAGE; 0001:P08499; -.
DR DNASU; 3343957; -.
DR GeneID; 58309957; -.
DR KEGG; cgb:cg1337; -.
DR KEGG; cgl:Cgl1183; -.
DR PATRIC; fig|196627.13.peg.1162; -.
DR eggNOG; COG0460; Bacteria.
DR HOGENOM; CLU_009116_1_0_11; -.
DR OMA; LMFYGPG; -.
DR BRENDA; 1.1.1.3; 960.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000000582; 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 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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW Reference proteome; Threonine biosynthesis.
FT CHAIN 1..445
FT /note="Homoserine dehydrogenase"
FT /id="PRO_0000066693"
FT DOMAIN 368..445
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 24..31
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 378
FT /note="G -> E (in FBR mutant)"
SQ SEQUENCE 445 AA; 46438 MW; 02731E502303CB1C CRC64;
MTSASAPSFN PGKGPGSAVG IALLGFGTVG TEVMRLMTEY GDELAHRIGG PLEVRGIAVS
DISKPREGVA PELLTEDAFA LIEREDVDIV VEVIGGIEYP REVVLAALKA GKSVVTANKA
LVAAHSAELA DAAEAANVDL YFEAAVAGAI PVVGPLRRSL AGDQIQSVMG IVNGTTNFIL
DAMDSTGADY ADSLAEATRL GYAEADPTAD VEGHDAASKA AILASIAFHT RVTADDVYCE
GISNISAADI EAAQQAGHTI KLLAICEKFT NKEGKSAISA RVHPTLLPVS HPLASVNKSF
NAIFVEAEAA GRLMFYGNGA GGAPTASAVL GDVVGAARNK VHGGRAPGES TYANLPIADF
GETTTRYHLD MDVEDRVGVL AELASLFSEQ GISLRTIRQE ERDDDARLIV VTHSALESDL
SRTVELLKAK PVVKAINSVI RLERD
