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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.2 Publications

Catalytic activityi

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH.2 Publications

Enzyme regulationi

Is inhibited by L- and D-cystine, and by other cystine derivatives, via the formation of a covalently bound cysteine at the active site Cys-135.1 Publication

Kineticsi

  1. KM=22 µM for L-4-aspartyl phosphate1 Publication
  2. KM=29 µM for NADPH1 Publication
  3. KM=110 µM for L-aspartate 4-semialdehyde1 Publication
  4. KM=144 µM for NADP+1 Publication
  5. KM=10.2 mM for phosphate1 Publication

    Pathwayi: L-lysine biosynthesis via DAP pathway

    This protein is involved in step 2 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.UniRule annotation
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Lysine-sensitive aspartokinase 3 (lysC), Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
    4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
    This subpathway is part of the pathway L-lysine biosynthesis via DAP 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 (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

    Pathwayi: L-methionine biosynthesis via de novo pathway

    This protein is involved in step 2 of the subpathway that synthesizes L-homoserine from L-aspartate.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
    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 2 of the subpathway that synthesizes L-threonine from L-aspartate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
    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 sitei73 – 731NADP1 Publication
    Binding sitei102 – 1021PhosphateUniRule annotation
    Active sitei135 – 1351Acyl-thioester intermediate1 Publication
    Binding sitei162 – 1621Substrate1 Publication
    Binding sitei173 – 1731NADP1 Publication
    Binding sitei193 – 1931NADP; via carbonyl oxygen1 Publication
    Binding sitei241 – 2411Substrate1 Publication
    Binding sitei244 – 2441PhosphateUniRule annotation
    Binding sitei267 – 2671Substrate1 Publication
    Active sitei274 – 2741Proton acceptor1 Publication
    Binding sitei350 – 3501NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 134NADP1 Publication
    Nucleotide bindingi37 – 382NADP1 Publication
    Nucleotide bindingi165 – 1695NADP1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis, Methionine biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MONOMER.
    ECOL316407:JW3396-MONOMER.
    MetaCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MONOMER.
    BRENDAi1.2.1.11. 2026.
    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate-semialdehyde dehydrogenaseUniRule annotation (EC:1.2.1.112 Publications)
    Short name:
    ASA dehydrogenaseUniRule annotation
    Short name:
    ASADHUniRule annotation
    Alternative name(s):
    Aspartate-beta-semialdehyde dehydrogenaseUniRule annotation
    Gene namesi
    Name:asdUniRule annotation
    Synonyms:hom
    Ordered Locus Names:b3433, JW3396
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10088. asd.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1351C → A: Complete loss of activity. 1 Publication
    Mutagenesisi135 – 1351C → S: 99.7% loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 367367Aspartate-semialdehyde dehydrogenasePRO_0000141369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei135 – 1351S-cysteinyl cysteine; in inhibited form

    Proteomic databases

    EPDiP0A9Q9.
    PaxDbiP0A9Q9.
    PRIDEiP0A9Q9.

    2D gel databases

    SWISS-2DPAGEP0A9Q9.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    IntActiP0A9Q9. 1 interaction.
    STRINGi511145.b3433.

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Helixi12 – 2312Combined sources
    Helixi26 – 294Combined sources
    Beta strandi30 – 3910Combined sources
    Beta strandi41 – 433Combined sources
    Helixi46 – 483Combined sources
    Helixi60 – 645Combined sources
    Beta strandi67 – 715Combined sources
    Helixi75 – 8713Combined sources
    Beta strandi93 – 964Combined sources
    Turni100 – 1034Combined sources
    Beta strandi107 – 1104Combined sources
    Helixi112 – 12413Combined sources
    Beta strandi129 – 1324Combined sources
    Helixi135 – 14915Combined sources
    Beta strandi153 – 16210Combined sources
    Helixi164 – 1663Combined sources
    Helixi169 – 18517Combined sources
    Helixi187 – 1904Combined sources
    Helixi197 – 21014Combined sources
    Turni216 – 2183Combined sources
    Beta strandi226 – 2283Combined sources
    Beta strandi235 – 2395Combined sources
    Helixi240 – 25314Combined sources
    Beta strandi261 – 2644Combined sources
    Beta strandi267 – 2693Combined sources
    Beta strandi271 – 28414Combined sources
    Helixi288 – 29811Combined sources
    Beta strandi302 – 3043Combined sources
    Helixi309 – 3157Combined sources
    Helixi318 – 3214Combined sources
    Beta strandi329 – 3346Combined sources
    Beta strandi341 – 3499Combined sources
    Helixi352 – 3565Combined sources
    Helixi357 – 36610Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BRMX-ray2.50A/B/C1-367[»]
    1GL3X-ray2.60A/B1-367[»]
    1T4BX-ray1.60A/B1-367[»]
    1T4DX-ray1.95A/B/C1-367[»]
    ProteinModelPortaliP0A9Q9.
    SMRiP0A9Q9. Positions 1-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9Q9.

    Family & Domainsi

    Domaini

    Consists of two domains, an N-terminal nucleotide-binding domain and a C-terminal dimerization domain.1 Publication

    Sequence similaritiesi

    Belongs to the aspartate-semialdehyde dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CM3. Bacteria.
    COG0136. LUCA.
    HOGENOMiHOG000161376.
    InParanoidiP0A9Q9.
    KOiK00133.
    OMAiSCQGGDY.
    PhylomeDBiP0A9Q9.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_02121. ASADH. 1 hit.
    InterProiIPR000319. Asp-semialdehyde_DH_CS.
    IPR011534. Asp_ADH_gamma-type.
    IPR012080. Asp_semialdehyde_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR000534. Semialdehyde_DH_NAD-bd.
    IPR012280. Semialdhyde_DH_dimer_dom.
    [Graphical view]
    PfamiPF01118. Semialdhyde_dh. 1 hit.
    PF02774. Semialdhyde_dhC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000148. ASA_dh. 1 hit.
    SMARTiSM00859. Semialdhyde_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01745. asd_gamma. 1 hit.
    PROSITEiPS01103. ASD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A9Q9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQL GQAAPSFGGT
    60 70 80 90 100
    TGTLQDAFDL EALKALDIIV TCQGGDYTNE IYPKLRESGW QGYWIDAASS
    110 120 130 140 150
    LRMKDDAIII LDPVNQDVIT DGLNNGIRTF VGGNCTVSLM LMSLGGLFAN
    160 170 180 190 200
    DLVDWVSVAT YQAASGGGAR HMRELLTQMG HLYGHVADEL ATPSSAILDI
    210 220 230 240 250
    ERKVTTLTRS GELPVDNFGV PLAGSLIPWI DKQLDNGQSR EEWKGQAETN
    260 270 280 290 300
    KILNTSSVIP VDGLCVRVGA LRCHSQAFTI KLKKDVSIPT VEELLAAHNP
    310 320 330 340 350
    WAKVVPNDRE ITMRELTPAA VTGTLTTPVG RLRKLNMGPE FLSAFTVGDQ
    360
    LLWGAAEPLR RMLRQLA
    Length:367
    Mass (Da):40,018
    Last modified:July 21, 1986 - v1
    Checksum:iF53D4C36EA7CC201
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91W → G AA sequence (PubMed:9298646).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00262 Genomic DNA. Translation: CAA23511.1.
    U18997 Genomic DNA. Translation: AAA58231.1.
    U00096 Genomic DNA. Translation: AAC76458.1.
    AP009048 Genomic DNA. Translation: BAE77859.1.
    PIRiA00364. DEECDA.
    RefSeqiNP_417891.1. NC_000913.3.
    WP_000799956.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76458; AAC76458; b3433.
    BAE77859; BAE77859; BAE77859.
    GeneIDi947939.
    KEGGiecj:JW3396.
    eco:b3433.
    PATRICi32122306. VBIEscCol129921_3530.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00262 Genomic DNA. Translation: CAA23511.1.
    U18997 Genomic DNA. Translation: AAA58231.1.
    U00096 Genomic DNA. Translation: AAC76458.1.
    AP009048 Genomic DNA. Translation: BAE77859.1.
    PIRiA00364. DEECDA.
    RefSeqiNP_417891.1. NC_000913.3.
    WP_000799956.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BRMX-ray2.50A/B/C1-367[»]
    1GL3X-ray2.60A/B1-367[»]
    1T4BX-ray1.60A/B1-367[»]
    1T4DX-ray1.95A/B/C1-367[»]
    ProteinModelPortaliP0A9Q9.
    SMRiP0A9Q9. Positions 1-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP0A9Q9. 1 interaction.
    STRINGi511145.b3433.

    2D gel databases

    SWISS-2DPAGEP0A9Q9.

    Proteomic databases

    EPDiP0A9Q9.
    PaxDbiP0A9Q9.
    PRIDEiP0A9Q9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76458; AAC76458; b3433.
    BAE77859; BAE77859; BAE77859.
    GeneIDi947939.
    KEGGiecj:JW3396.
    eco:b3433.
    PATRICi32122306. VBIEscCol129921_3530.

    Organism-specific databases

    EchoBASEiEB0086.
    EcoGeneiEG10088. asd.

    Phylogenomic databases

    eggNOGiENOG4105CM3. Bacteria.
    COG0136. LUCA.
    HOGENOMiHOG000161376.
    InParanoidiP0A9Q9.
    KOiK00133.
    OMAiSCQGGDY.
    PhylomeDBiP0A9Q9.

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.
    BioCyciEcoCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MONOMER.
    ECOL316407:JW3396-MONOMER.
    MetaCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MONOMER.
    BRENDAi1.2.1.11. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A9Q9.
    PROiP0A9Q9.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_02121. ASADH. 1 hit.
    InterProiIPR000319. Asp-semialdehyde_DH_CS.
    IPR011534. Asp_ADH_gamma-type.
    IPR012080. Asp_semialdehyde_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR000534. Semialdehyde_DH_NAD-bd.
    IPR012280. Semialdhyde_DH_dimer_dom.
    [Graphical view]
    PfamiPF01118. Semialdhyde_dh. 1 hit.
    PF02774. Semialdhyde_dhC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000148. ASA_dh. 1 hit.
    SMARTiSM00859. Semialdhyde_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01745. asd_gamma. 1 hit.
    PROSITEiPS01103. ASD. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHAS_ECOLI
    AccessioniPrimary (citable) accession number: P0A9Q9
    Secondary accession number(s): P00353, Q2M797
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: September 7, 2016
    This is version 106 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.