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Protein

Homoserine dehydrogenase

Gene

hom

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.2 Publications

Enzyme regulationi

Feedback inhibition by threonine.2 Publications

Kineticsi

  1. KM=190 µM for L-aspartate 4-semialdehyde1 Publication
  2. KM=37.4 µM for NADPH1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Pathwayi: L-methionine biosynthesis via de novo pathway

    This protein is involved in step 3 of the subpathway that synthesizes L-homoserine from L-aspartate.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Aspartokinase (lysC)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Homoserine dehydrogenase (hom)
    This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

    Pathwayi: L-threonine biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes L-threonine from L-aspartate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Aspartokinase (lysC)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Homoserine dehydrogenase (hom)
    4. Homoserine kinase (thrB)
    5. Threonine synthase (thrC)
    This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191NADPBy similarity
    Binding sitei204 – 2041SubstrateBy similarity
    Active sitei219 – 2191Proton donorSequence analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi24 – 318NADPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis, Methionine biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00050; UER00063.
    UPA00051; UER00465.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homoserine dehydrogenase (EC:1.1.1.3)
    Short name:
    HDH
    Gene namesi
    Name:hom
    Synonyms:thrA
    Ordered Locus Names:Cgl1183, cg1337
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
    Proteomesi
    • UP000000582 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Homoserine dehydrogenasePRO_0000066693Add
    BLAST

    Proteomic databases

    PRIDEiP08499.

    2D gel databases

    World-2DPAGE0001:P08499.

    Interactioni

    Protein-protein interaction databases

    STRINGi196627.cg1337.

    Structurei

    3D structure databases

    ProteinModelPortaliP08499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini368 – 44578ACTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the homoserine dehydrogenase family.Curated
    Contains 1 ACT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4105D6E. Bacteria.
    COG0460. LUCA.
    HOGENOMiHOG000076615.
    KOiK00003.
    OMAiEWIAGII.
    OrthoDBiEOG6XM7CQ.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR005106. Asp/hSer_DH_NAD-bd.
    IPR016204. HDH.
    IPR001342. HDH_cat.
    IPR019811. HDH_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01842. ACT. 1 hit.
    PF00742. Homoserine_dh. 1 hit.
    PF03447. NAD_binding_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000098. Homoser_dehydrog. 1 hit.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS01042. HOMOSER_DHGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08499-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSASAPSFN PGKGPGSAVG IALLGFGTVG TEVMRLMTEY GDELAHRIGG
    60 70 80 90 100
    PLEVRGIAVS DISKPREGVA PELLTEDAFA LIEREDVDIV VEVIGGIEYP
    110 120 130 140 150
    REVVLAALKA GKSVVTANKA LVAAHSAELA DAAEAANVDL YFEAAVAGAI
    160 170 180 190 200
    PVVGPLRRSL AGDQIQSVMG IVNGTTNFIL DAMDSTGADY ADSLAEATRL
    210 220 230 240 250
    GYAEADPTAD VEGHDAASKA AILASIAFHT RVTADDVYCE GISNISAADI
    260 270 280 290 300
    EAAQQAGHTI KLLAICEKFT NKEGKSAISA RVHPTLLPVS HPLASVNKSF
    310 320 330 340 350
    NAIFVEAEAA GRLMFYGNGA GGAPTASAVL GDVVGAARNK VHGGRAPGES
    360 370 380 390 400
    TYANLPIADF GETTTRYHLD MDVEDRVGVL AELASLFSEQ GISLRTIRQE
    410 420 430 440
    ERDDDARLIV VTHSALESDL SRTVELLKAK PVVKAINSVI RLERD
    Length:445
    Mass (Da):46,438
    Last modified:August 1, 1988 - v1
    Checksum:i02731E502303CB1C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti378 – 3781G → E in FBR mutant.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y00546 Genomic DNA. Translation: CAA68614.1.
    Y00476 Genomic DNA. Translation: CAA68536.1.
    BA000036 Genomic DNA. Translation: BAB98576.1.
    BX927151 Genomic DNA. Translation: CAF19887.1.
    PIRiS00865. DEFKHG.
    RefSeqiNP_600409.1. NC_003450.3.
    WP_003854900.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB98576; BAB98576; BAB98576.
    CAF19887; CAF19887; cg1337.
    GeneIDi1019166.
    KEGGicgb:cg1337.
    cgl:NCgl1136.
    PATRICi21494412. VBICorGlu203724_1162.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y00546 Genomic DNA. Translation: CAA68614.1.
    Y00476 Genomic DNA. Translation: CAA68536.1.
    BA000036 Genomic DNA. Translation: BAB98576.1.
    BX927151 Genomic DNA. Translation: CAF19887.1.
    PIRiS00865. DEFKHG.
    RefSeqiNP_600409.1. NC_003450.3.
    WP_003854900.1. NC_006958.1.

    3D structure databases

    ProteinModelPortaliP08499.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi196627.cg1337.

    2D gel databases

    World-2DPAGE0001:P08499.

    Proteomic databases

    PRIDEiP08499.

    Protocols and materials databases

    DNASUi3343957.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB98576; BAB98576; BAB98576.
    CAF19887; CAF19887; cg1337.
    GeneIDi1019166.
    KEGGicgb:cg1337.
    cgl:NCgl1136.
    PATRICi21494412. VBICorGlu203724_1162.

    Phylogenomic databases

    eggNOGiENOG4105D6E. Bacteria.
    COG0460. LUCA.
    HOGENOMiHOG000076615.
    KOiK00003.
    OMAiEWIAGII.
    OrthoDBiEOG6XM7CQ.

    Enzyme and pathway databases

    UniPathwayiUPA00050; UER00063.
    UPA00051; UER00465.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR005106. Asp/hSer_DH_NAD-bd.
    IPR016204. HDH.
    IPR001342. HDH_cat.
    IPR019811. HDH_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01842. ACT. 1 hit.
    PF00742. Homoserine_dh. 1 hit.
    PF03447. NAD_binding_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000098. Homoser_dehydrog. 1 hit.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS01042. HOMOSER_DHGENASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence and fine structural analysis of the Corynebacterium glutamicum hom-thrB operon."
      Peoples O.P., Liebl W., Bodis M., Maeng P.J., Follettie M.T., Archer J.A.C., Sinskey A.J.
      Mol. Microbiol. 2:63-72(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
    2. "Nucleotide sequence of the homoserine dehydrogenase (thr A) gene of Brevibacterium lactofermentum."
      Mateos L.M., del Real G., Aguilar A., Martin J.F.
      Nucleic Acids Res. 15:10598-10598(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Sequence analysis of functional regions of homoserine dehydrogenase genes from L-lysine and L-threonine-producing mutants of Brevibacterium lactofermentum."
      Sugimoto M., Tanaka A., Suzuki T., Matsui H., Nakamori S., Takagi H.
      Biosci. Biotechnol. Biochem. 61:1760-1762(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    6. "Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. 3. Properties of homoserine dehydrogenase."
      Miyajima R., Shiio I.
      J. Biochem. 68:311-319(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "A C-terminal deletion in Corynebacterium glutamicum homoserine dehydrogenase abolishes allosteric inhibition by L-threonine."
      Archer J.A., Solow-Cordero D.E., Sinskey A.J.
      Gene 107:53-59(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
    8. "Analysis of a Corynebacterium glutamicum hom gene coding for a feedback-resistant homoserine dehydrogenase."
      Reinscheid D.J., Eikmanns B.J., Sahm H.
      J. Bacteriol. 173:3228-3230(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANT RESISTANT TO FEEDBACK INHIBITION (FBR).

    Entry informationi

    Entry nameiDHOM_CORGL
    AccessioniPrimary (citable) accession number: P08499
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: December 9, 2015
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.