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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

Kineticsi

  1. KM=0.12 mM for L-aspartate 4-semialdehyde1 Publication
  2. KM=0.13 mM for NADP+1 Publication
  3. KM=1.5 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.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Aspartokinase (lysC)
    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.
    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 2 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 sitei73 – 731NADPBy similarity
    Binding sitei102 – 1021PhosphateBy similarity
    Active sitei135 – 1351Acyl-thioester intermediateBy similarity
    Binding sitei162 – 1621SubstrateBy similarity
    Binding sitei193 – 1931NADP; via carbonyl oxygenBy similarity
    Binding sitei241 – 2411SubstrateBy similarity
    Binding sitei244 – 2441PhosphateBy similarity
    Binding sitei268 – 2681SubstrateBy similarity
    Active sitei275 – 2751Proton acceptorBy similarity
    Binding sitei351 – 3511NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 134NADPBy similarity
    Nucleotide bindingi37 – 382NADPBy similarity
    Nucleotide bindingi165 – 1662NADPBy similarity

    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. 5087.
    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate-semialdehyde dehydrogenase (EC:1.2.1.11)
    Short name:
    ASA dehydrogenase
    Short name:
    ASADH
    Alternative name(s):
    Aspartate-beta-semialdehyde dehydrogenase
    Gene namesi
    Name:asd
    Ordered Locus Names:PA3117
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA3117.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Aspartate-semialdehyde dehydrogenasePRO_0000141387Add
    BLAST

    Proteomic databases

    PaxDbiQ51344.
    PRIDEiQ51344.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi208964.PA3117.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Helixi12 – 2312Combined sources
    Helixi26 – 283Combined sources
    Beta strandi29 – 3810Combined sources
    Helixi60 – 634Combined sources
    Beta strandi67 – 715Combined sources
    Helixi75 – 8713Combined sources
    Beta strandi92 – 998Combined sources
    Turni100 – 1034Combined sources
    Beta strandi107 – 1104Combined sources
    Helixi112 – 12514Combined sources
    Beta strandi129 – 1324Combined sources
    Helixi135 – 14915Combined sources
    Beta strandi153 – 16210Combined sources
    Helixi164 – 1663Combined sources
    Helixi169 – 18416Combined sources
    Helixi187 – 1915Combined sources
    Helixi197 – 20913Combined sources
    Turni216 – 2183Combined sources
    Helixi240 – 25213Combined sources
    Beta strandi262 – 2687Combined sources
    Beta strandi270 – 28516Combined sources
    Helixi289 – 2979Combined sources
    Beta strandi301 – 3055Combined sources
    Helixi310 – 3167Combined sources
    Helixi319 – 3224Combined sources
    Beta strandi328 – 3358Combined sources
    Beta strandi342 – 3509Combined sources
    Helixi353 – 3575Combined sources
    Helixi358 – 36811Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5BNTX-ray2.10A/B/C/D1-370[»]
    ProteinModelPortaliQ51344.
    SMRiQ51344. Positions 1-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CM3. Bacteria.
    COG0136. LUCA.
    HOGENOMiHOG000161376.
    InParanoidiQ51344.
    KOiK00133.
    OMAiSCQGGDY.
    PhylomeDBiQ51344.

    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.

    Q51344-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKRVGLIGWR GMVGSVLMQR MLEERDFDLI EPVFFTTSNV GGQGPEVGKD
    60 70 80 90 100
    IAPLKDAYSI DELKTLDVIL TCQGGDYTSE VFPKLREAGW QGYWIDAASS
    110 120 130 140 150
    LRMEDDAVIV LDPVNRKVID QALDAGTRNY IGGNCTVSLM LMALGGLFDA
    160 170 180 190 200
    GLVEWMSAMT YQAASGAGAQ NMRELLKQMG AAHASVADDL ANPASAILDI
    210 220 230 240 250
    DRKVAETLRS EAFPTEHFGA PLGGSLIPWI DKELPNGQSR EEWKAQAETN
    260 270 280 290 300
    KILARFKNPI PVDGICVRVG AMRCHSQALT IKLNKDVPLT DIEGLISQHN
    310 320 330 340 350
    PWVKLVPNHR EVSVRELTPA AVTGTLSVPV GRLRKLNMGS QYLGAFTVGD
    360 370
    QLLWGAAEPL RRMLRILLER
    Length:370
    Mass (Da):40,495
    Last modified:December 8, 2000 - v2
    Checksum:i03E66CF12FA9A378
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181M → I in AAB51626 (PubMed:9084174).Curated
    Sequence conflicti42 – 443GQG → AQA in AAB51626 (PubMed:9084174).Curated
    Sequence conflicti48 – 481G → D in AAB51626 (PubMed:9084174).Curated
    Sequence conflicti174 – 1741E → D in AAB51626 (PubMed:9084174).Curated
    Sequence conflicti235 – 2373PNG → SQRR in AAB51626 (PubMed:9084174).Curated
    Sequence conflicti297 – 2971S → R in AAB51626 (PubMed:9084174).Curated
    Sequence conflicti339 – 3391G → V in AAB51626 (PubMed:9084174).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U11055 Genomic DNA. Translation: AAB51626.1.
    AE004091 Genomic DNA. Translation: AAG06505.1.
    PIRiC83255.
    RefSeqiNP_251807.1. NC_002516.2.
    WP_003111187.1. NZ_ASJY01000511.1.

    Genome annotation databases

    EnsemblBacteriaiAAG06505; AAG06505; PA3117.
    GeneIDi882803.
    KEGGipae:PA3117.
    PATRICi19840807. VBIPseAer58763_3269.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U11055 Genomic DNA. Translation: AAB51626.1.
    AE004091 Genomic DNA. Translation: AAG06505.1.
    PIRiC83255.
    RefSeqiNP_251807.1. NC_002516.2.
    WP_003111187.1. NZ_ASJY01000511.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5BNTX-ray2.10A/B/C/D1-370[»]
    ProteinModelPortaliQ51344.
    SMRiQ51344. Positions 1-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA3117.

    Proteomic databases

    PaxDbiQ51344.
    PRIDEiQ51344.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG06505; AAG06505; PA3117.
    GeneIDi882803.
    KEGGipae:PA3117.
    PATRICi19840807. VBIPseAer58763_3269.

    Organism-specific databases

    PseudoCAPiPA3117.

    Phylogenomic databases

    eggNOGiENOG4105CM3. Bacteria.
    COG0136. LUCA.
    HOGENOMiHOG000161376.
    InParanoidiQ51344.
    KOiK00133.
    OMAiSCQGGDY.
    PhylomeDBiQ51344.

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.
    BRENDAi1.2.1.11. 5087.

    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_PSEAE
    AccessioniPrimary (citable) accession number: Q51344
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 8, 2000
    Last modified: September 7, 2016
    This is version 110 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.