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 04-NOV-2008, entry version 68. 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 (Brevibacterium flavum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1718; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613; RX MEDLINE=88216182; PubMed=2835591; 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 RT Corynebacterium glutamicum hom-thrB operon."; RL Mol. Microbiol. 2:63-72(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88096601; 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 MEDLINE=98028217; PubMed=9362124; RA Sugimoto M., Tanaka A., Suzuki T., Matsui H., Nakamori S., Takagi H.; RT "Sequence analysis of functional regions of homoserine dehydrogenase RT genes from L-lysine and L-threonine-producing mutants of RT Brevibacterium lactofermentum."; RL Biosci. Biotechnol. Biochem. 61:1760-1762(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). RN [6] RP MUTANT RESISTANT TO FEEDBACK INHIBITION (FBR). RX MEDLINE=91216997; PubMed=1902466; RA Reinscheid D.J., Eikmanns B.J., Sahm H.; RT "Analysis of a Corynebacterium glutamicum hom gene coding for a RT feedback-resistant homoserine dehydrogenase."; RL J. Bacteriol. 173:3228-3230(1991). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. CC -!- ENZYME REGULATION: Feedback inhibition by threonine. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 3/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 3/5. CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family. CC -!- SIMILARITY: Contains 1 ACT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; -. DR RefSeq; YP_225473.1; -. DR World-2DPAGE; 0001:P08499; -. DR GeneID; 1019166; -. DR GeneID; 3343957; -. DR GenomeReviews; BX927147_GR; cg1337. DR GenomeReviews; BA000036_GR; Cgl1183. DR KEGG; cgb:cg1337; -. DR KEGG; cgl:NCgl1136; -. DR HOGENOM; P08499; -. DR BioCyc; CGLU196627-1:CG1337-MON; -. 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR002912; ACT_bd. DR InterPro; IPR005106; Asp/hSer_DHase_NAD-bd. DR InterPro; IPR016204; hSer_DHase. DR InterPro; IPR001342; hSer_DHase_cat. 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 PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Isoleucine biosynthesis; Methionine biosynthesis; KW NADP; Oxidoreductase; Threonine biosynthesis. FT CHAIN 1 445 Homoserine dehydrogenase. FT /FTId=PRO_0000066693. FT DOMAIN 367 439 ACT. FT NP_BIND 24 31 NADP (By similarity). FT ACT_SITE 219 219 Proton donor (Potential). FT BINDING 119 119 NADP (By similarity). FT BINDING 204 204 Substrate (By similarity). FT VARIANT 378 378 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 //