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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)DescriptionActionsGraphical viewLength
    Binding sitei74NADP1 Publication1
    Binding sitei103Phosphate1 Publication1
    Active sitei136Acyl-thioester intermediate2 Publications1
    Binding sitei163Substrate1 Publication1
    Binding sitei166NADP; via carbonyl oxygen1 Publication1
    Binding sitei243Substrate1 Publication1
    Binding sitei246Phosphate1 Publication1
    Binding sitei270Substrate1 Publication1
    Active sitei277Proton acceptor1 Publication1
    Binding sitei353NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi10 – 13NADP1 Publication4
    Nucleotide bindingi37 – 38NADP1 Publication2

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi103R → K: 2-fold increase in affinity for ASA, 23-fold decrease in affinity for phosphate, and 275-fold decrease in activity. 1 Publication1
    Mutagenesisi103R → L: 7-fold increase in affinity for ASA, 150-fold decrease in affinity for phosphate, and 1400-fold decrease in activity. 1 Publication1
    Mutagenesisi243E → D: No change in affinity for ASA and 82-fold decrease in activity. 1 Publication1
    Mutagenesisi246K → R: 2-fold increase in affinity for ASA, nearly no change in affinity for phosphate, and 30-fold decrease in activity. 1 Publication1
    Mutagenesisi270R → K: 2-fold decrease in affinity for ASA and 825-fold decrease in activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001413751 – 371Aspartate-semialdehyde dehydrogenaseAdd BLAST371

    Proteomic databases

    PRIDEiP44801.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi71421.HI0646.

    Structurei

    Secondary structure

    1371
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 8Combined sources7
    Helixi12 – 24Combined sources13
    Turni25 – 29Combined sources5
    Beta strandi30 – 38Combined sources9
    Helixi47 – 49Combined sources3
    Helixi61 – 64Combined sources4
    Beta strandi68 – 72Combined sources5
    Helixi76 – 88Combined sources13
    Beta strandi93 – 100Combined sources8
    Turni101 – 104Combined sources4
    Beta strandi108 – 111Combined sources4
    Helixi113 – 126Combined sources14
    Beta strandi130 – 133Combined sources4
    Helixi136 – 150Combined sources15
    Beta strandi154 – 163Combined sources10
    Helixi165 – 167Combined sources3
    Helixi170 – 185Combined sources16
    Helixi188 – 191Combined sources4
    Helixi198 – 209Combined sources12
    Turni217 – 219Combined sources3
    Beta strandi225 – 228Combined sources4
    Turni236 – 238Combined sources3
    Helixi242 – 255Combined sources14
    Beta strandi258 – 260Combined sources3
    Beta strandi264 – 267Combined sources4
    Beta strandi270 – 287Combined sources18
    Helixi291 – 300Combined sources10
    Beta strandi303 – 307Combined sources5
    Helixi312 – 318Combined sources7
    Helixi321 – 324Combined sources4
    Beta strandi330 – 338Combined sources9
    Beta strandi341 – 352Combined sources12
    Turni353 – 358Combined sources6
    Helixi359 – 370Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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
    PDB 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.
    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: November 2, 2016
    This is version 125 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.