ID DHOM_HELPJ Reviewed; 421 AA. AC Q9ZL20; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 25-NOV-2008, entry version 52. DE RecName: Full=Homoserine dehydrogenase; DE Short=HDH; DE EC=1.1.1.3; GN Name=hom; OrderedLocusNames=jhp_0761; OS Helicobacter pylori J99 (Campylobacter pylori J99). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=99120557; PubMed=9923682; DOI=10.1038/16495; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., RA Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., RA Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., RA Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human RT gastric pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. 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; AE001439; AAD06338.1; -; Genomic_DNA. DR PIR; C71893; C71893. DR RefSeq; NP_223479.1; -. DR GeneID; 890134; -. DR GenomeReviews; AE001439_GR; jhp_0761. DR KEGG; hpj:jhp0761; -. DR NMPDR; fig|85963.1.peg.757; -. DR HOGENOM; Q9ZL20; -. DR BioCyc; HPYL85963:JHP0761-MON; -. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004412; F:homoserine dehydrogenase activity; 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: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 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Isoleucine biosynthesis; Methionine biosynthesis; KW NADP; Oxidoreductase; Threonine biosynthesis. FT CHAIN 1 421 Homoserine dehydrogenase. FT /FTId=PRO_0000066695. FT DOMAIN 342 419 ACT. FT NP_BIND 10 17 NADP (By similarity). FT ACT_SITE 201 201 Proton donor (Potential). FT BINDING 103 103 NADP (By similarity). FT BINDING 186 186 Substrate (By similarity). SQ SEQUENCE 421 AA; 46247 MW; 4DC5921EB61D4A78 CRC64; MKKRLNIGLV GLGCVGSTVA KILQENQEII KDRAGVEIKI KKAVVRDVKK HKGYAFEISD DLESVIEDKG IDIVVELMGG VEAPYLLAKK TLAKQKAFVT ANKAMLAYHR YELEQIAKNT PIGFEASVCG GIPIIKALKD GLSANHILSF KGILNGTSNY ILSQMFKNQA SFKDALKDAQ HLGYAELNPE FDIKGIDAAH KLLILASLAY GIDAKLEEIL IEGIEKIEPD DMEFAKEFGY SIKLLGIAKK HQDCIELRVH PSMIKNECML SKVDGVMNAI SVIGDKVGET LYYGAGAGGE PTASAVISDI IEIARKKSSL MLGFETPQKL PLKPKEEIQC AYYARLLVSD EKGVFSQISA ILAQNDISLN NVLQKEIPQS NKAKILFSTH TTNEKSMLNA LKELENLQSV LDTPKMIRLE N //