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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.24 mM for L-aspartate 4-semialdehyde1 Publication
  2. KM=0.15 mM for NADP+1 Publication
  3. KM=1.6 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. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    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 (thrA)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    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 (thrA)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    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 sitei74 – 741NADP1 Publication
    Binding sitei103 – 1031Phosphate1 Publication
    Active sitei136 – 1361Acyl-thioester intermediate2 Publications
    Binding sitei163 – 1631Substrate1 Publication
    Binding sitei166 – 1661NADP; via carbonyl oxygen1 Publication
    Binding sitei243 – 2431Substrate1 Publication
    Binding sitei246 – 2461Phosphate1 Publication
    Binding sitei270 – 2701Substrate1 Publication
    Active sitei277 – 2771Proton acceptor1 Publication
    Binding sitei353 – 3531NADP1 Publication

    Regions

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

    BRENDAi1.2.1.11. 2529.
    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
    Ordered Locus Names:HI_0646
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    Proteomesi
    • UP000000579 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031R → K: 2-fold increase in affinity for ASA, 23-fold decrease in affinity for phosphate, and 275-fold decrease in activity. 1 Publication
    Mutagenesisi103 – 1031R → L: 7-fold increase in affinity for ASA, 150-fold decrease in affinity for phosphate, and 1400-fold decrease in activity. 1 Publication
    Mutagenesisi243 – 2431E → D: No change in affinity for ASA and 82-fold decrease in activity. 1 Publication
    Mutagenesisi246 – 2461K → R: 2-fold increase in affinity for ASA, nearly no change in affinity for phosphate, and 30-fold decrease in activity. 1 Publication
    Mutagenesisi270 – 2701R → K: 2-fold decrease in affinity for ASA and 825-fold decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 371371Aspartate-semialdehyde dehydrogenasePRO_0000141375Add
    BLAST

    Proteomic databases

    PRIDEiP44801.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi71421.HI0646.

    Structurei

    Secondary structure

    1
    371
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87Combined sources
    Helixi12 – 2413Combined sources
    Turni25 – 295Combined sources
    Beta strandi30 – 389Combined sources
    Helixi47 – 493Combined sources
    Helixi61 – 644Combined sources
    Beta strandi68 – 725Combined sources
    Helixi76 – 8813Combined sources
    Beta strandi93 – 1008Combined sources
    Turni101 – 1044Combined sources
    Beta strandi108 – 1114Combined sources
    Helixi113 – 12614Combined sources
    Beta strandi130 – 1334Combined sources
    Helixi136 – 15015Combined sources
    Beta strandi154 – 16310Combined sources
    Helixi165 – 1673Combined sources
    Helixi170 – 18516Combined sources
    Helixi188 – 1914Combined sources
    Helixi198 – 20912Combined sources
    Turni217 – 2193Combined sources
    Beta strandi225 – 2284Combined sources
    Turni236 – 2383Combined sources
    Helixi242 – 25514Combined sources
    Beta strandi258 – 2603Combined sources
    Beta strandi264 – 2674Combined sources
    Beta strandi270 – 28718Combined sources
    Helixi291 – 30010Combined sources
    Beta strandi303 – 3075Combined sources
    Helixi312 – 3187Combined sources
    Helixi321 – 3244Combined sources
    Beta strandi330 – 3389Combined sources
    Beta strandi341 – 35212Combined sources
    Turni353 – 3586Combined sources
    Helixi359 – 37012Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NWCX-ray2.04A/B1-371[»]
    1NWHX-ray2.00A/B1-371[»]
    1NX6X-ray2.15A1-371[»]
    1OZAX-ray2.06A1-371[»]
    1PQPX-ray2.06A1-371[»]
    1PQUX-ray1.92A/B/C/D1-371[»]
    1PR3X-ray2.15A1-371[»]
    1PS8X-ray2.40A1-371[»]
    1PU2X-ray2.06A1-371[»]
    1Q2XX-ray2.05A/B1-371[»]
    1TA4X-ray2.28A1-371[»]
    1TB4X-ray2.15A1-371[»]
    ProteinModelPortaliP44801.
    SMRiP44801. Positions 1-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP44801.

    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.
    KOiK00133.
    OMAiSCQGGDY.
    PhylomeDBiP44801.

    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.

    P44801-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKNVGFIGWR GMVGSVLMDR MSQENDFENL NPVFFTTSQA GQKAPVFGGK
    60 70 80 90 100
    DAGDLKSAFD IEELKKLDII VTCQGGDYTN EVYPKLKATG WDGYWVDAAS
    110 120 130 140 150
    ALRMKDDAII VLDPVNQHVI SEGLKKGIKT FVGGNCTVSL MLMAIGGLFE
    160 170 180 190 200
    KDLVEWISVA TYQAASGAGA KNMRELLSQM GLLEQAVSSE LKDPASSILD
    210 220 230 240 250
    IERKVTAKMR ADNFPTDNFG AALGGSLIPW IDKLLPETGQ TKEEWKGYAE
    260 270 280 290 300
    TNKILGLSDN PIPVDGLCVR IGALRCHSQA FTIKLKKDLP LEEIEQIIAS
    310 320 330 340 350
    HNEWVKVIPN DKEITLRELT PAKVTGTLSV PVGRLRKLAM GPEYLAAFTV
    360 370
    GDQLLWGAAE PVRRILKQLV A
    Length:371
    Mass (Da):40,539
    Last modified:November 1, 1995 - v1
    Checksum:iE44CE5B90F2AF041
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L42023 Genomic DNA. Translation: AAC22306.1.
    PIRiB64084.
    RefSeqiNP_438806.1. NC_000907.1.
    WP_005694497.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC22306; AAC22306; HI_0646.
    GeneIDi949960.
    KEGGihin:HI0646.
    PATRICi20189907. VBIHaeInf48452_0675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L42023 Genomic DNA. Translation: AAC22306.1.
    PIRiB64084.
    RefSeqiNP_438806.1. NC_000907.1.
    WP_005694497.1. NC_000907.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NWCX-ray2.04A/B1-371[»]
    1NWHX-ray2.00A/B1-371[»]
    1NX6X-ray2.15A1-371[»]
    1OZAX-ray2.06A1-371[»]
    1PQPX-ray2.06A1-371[»]
    1PQUX-ray1.92A/B/C/D1-371[»]
    1PR3X-ray2.15A1-371[»]
    1PS8X-ray2.40A1-371[»]
    1PU2X-ray2.06A1-371[»]
    1Q2XX-ray2.05A/B1-371[»]
    1TA4X-ray2.28A1-371[»]
    1TB4X-ray2.15A1-371[»]
    ProteinModelPortaliP44801.
    SMRiP44801. Positions 1-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi71421.HI0646.

    Proteomic databases

    PRIDEiP44801.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC22306; AAC22306; HI_0646.
    GeneIDi949960.
    KEGGihin:HI0646.
    PATRICi20189907. VBIHaeInf48452_0675.

    Phylogenomic databases

    eggNOGiENOG4105CM3. Bacteria.
    COG0136. LUCA.
    KOiK00133.
    OMAiSCQGGDY.
    PhylomeDBiP44801.

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.
    BRENDAi1.2.1.11. 2529.

    Miscellaneous databases

    EvolutionaryTraceiP44801.

    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_HAEIN
    AccessioniPrimary (citable) accession number: P44801
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: September 7, 2016
    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    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.