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Protein

Aspartate-semialdehyde dehydrogenase 1

Gene

asd1

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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.1 Publication

Enzyme regulationi

Inhibited by S-methyl-L-cysteine sulfoxide in vitro, via the formation of a covalently bound cysteine at the active site Cys-134.1 Publication

Kineticsi

  1. KM=0.19 mM for L-aspartate 4-semialdehyde1 Publication
  2. KM=0.32 mM for NADP+1 Publication
  3. KM=1.1 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. Aspartokinase (VC_0547), Aspartokinase (VC_0391)
    2. Aspartate-semialdehyde dehydrogenase 1 (asd1), Aspartate-semialdehyde dehydrogenase 2 (asd2)
    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. Aspartokinase (VC_0547), Aspartokinase (VC_0391)
    2. Aspartate-semialdehyde dehydrogenase 1 (asd1), Aspartate-semialdehyde dehydrogenase 2 (asd2)
    3. no protein annotated in this organism
    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. Aspartokinase (VC_0547), Aspartokinase (VC_0391)
    2. Aspartate-semialdehyde dehydrogenase 1 (asd1), Aspartate-semialdehyde dehydrogenase 2 (asd2)
    3. no protein annotated in this organism
    4. Homoserine kinase (thrB)
    5. no protein annotated in this organism
    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 sitei72NADP1 Publication1
    Binding sitei101PhosphateUniRule annotation1
    Active sitei134Acyl-thioester intermediate1 Publication1
    Binding sitei161Substrate1 Publication1
    Binding sitei192NADP; via carbonyl oxygen1 Publication1
    Binding sitei240Substrate1 Publication1
    Binding sitei243PhosphateUniRule annotation1
    Binding sitei267Substrate1 Publication1
    Active sitei274Proton acceptor1 Publication1
    Binding sitei350NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi9 – 12NADP1 Publication4
    Nucleotide bindingi36 – 37NADP1 Publication2
    Nucleotide bindingi164 – 165NADP1 Publication2

    GO - Molecular functioni

    GO - Biological processi

    • 'de novo' L-methionine biosynthetic process Source: UniProtKB-HAMAP
    • diaminopimelate biosynthetic process Source: UniProtKB-HAMAP
    • isoleucine biosynthetic process Source: TIGR
    • lysine biosynthetic process via diaminopimelate Source: TIGR
    • methionine biosynthetic process Source: TIGR
    • threonine biosynthetic process Source: TIGR
    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

    BioCyciMetaCyc:MONOMER-15807.
    VCHO:VC2036-MONOMER.
    BRENDAi1.2.1.11. 6626.
    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate-semialdehyde dehydrogenase 1 (EC:1.2.1.111 Publication)
    Short name:
    ASA dehydrogenase 1
    Short name:
    ASADH 1
    Alternative name(s):
    Aspartate-beta-semialdehyde dehydrogenase 1
    Gene namesi
    Name:asd1
    Ordered Locus Names:VC_2036
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    Proteomesi
    • UP000000584 Componenti: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004111261 – 370Aspartate-semialdehyde dehydrogenase 1Add BLAST370

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei134S-cysteinyl cysteine; in inhibited form1

    Proteomic databases

    PRIDEiQ9KQG2.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi243277.VC2036.

    Structurei

    Secondary structure

    1370
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 7Combined sources6
    Helixi11 – 22Combined sources12
    Helixi25 – 28Combined sources4
    Beta strandi29 – 38Combined sources10
    Beta strandi40 – 42Combined sources3
    Beta strandi46 – 48Combined sources3
    Helixi59 – 62Combined sources4
    Beta strandi66 – 70Combined sources5
    Helixi74 – 86Combined sources13
    Beta strandi92 – 95Combined sources4
    Turni99 – 102Combined sources4
    Beta strandi106 – 109Combined sources4
    Helixi111 – 123Combined sources13
    Beta strandi128 – 131Combined sources4
    Helixi134 – 148Combined sources15
    Beta strandi152 – 161Combined sources10
    Helixi163 – 165Combined sources3
    Helixi168 – 190Combined sources23
    Helixi196 – 208Combined sources13
    Turni215 – 217Combined sources3
    Beta strandi224 – 227Combined sources4
    Beta strandi234 – 236Combined sources3
    Helixi239 – 251Combined sources13
    Beta strandi255 – 257Combined sources3
    Beta strandi267 – 269Combined sources3
    Beta strandi271 – 284Combined sources14
    Helixi288 – 296Combined sources9
    Beta strandi300 – 304Combined sources5
    Helixi309 – 315Combined sources7
    Helixi318 – 321Combined sources4
    Beta strandi327 – 335Combined sources9
    Beta strandi338 – 349Combined sources12
    Turni350 – 355Combined sources6
    Helixi356 – 369Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MB4X-ray1.84A/B1-370[»]
    1MC4X-ray2.77A1-370[»]
    3PZRX-ray1.75A/B1-370[»]
    3Q0EX-ray1.80A/B1-370[»]
    4R5MX-ray1.89A/B1-370[»]
    ProteinModelPortaliQ9KQG2.
    SMRiQ9KQG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9KQG2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aspartate-semialdehyde dehydrogenase family.UniRule annotation

    Phylogenomic databases

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

    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.

    Q9KQG2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVGLVGWRG MVGSVLMQRM VEERDFDLIE PVFFSTSQIG VPAPNFGKDA
    60 70 80 90 100
    GMLHDAFDIE SLKQLDAVIT CQGGSYTEKV YPALRQAGWK GYWIDAASTL
    110 120 130 140 150
    RMDKEAIITL DPVNLKQILH GIHHGTKTFV GGNCTVSLML MALGGLYERG
    160 170 180 190 200
    LVEWMSAMTY QAASGAGAQN MRELISQMGV INDAVSSELA NPASSILDID
    210 220 230 240 250
    KKVAETMRSG SFPTDNFGVP LAGSLIPWID VKRDNGQSKE EWKAGVEANK
    260 270 280 290 300
    ILGLQDSPVP IDGTCVRIGA MRCHSQALTI KLKQNIPLDE IEEMIATHND
    310 320 330 340 350
    WVKVIPNERD ITARELTPAK VTGTLSVPVG RLRKMAMGDD FLNAFTVGDQ
    360 370
    LLWGAAEPLR RTLRIILAEK
    Length:370
    Mass (Da):40,498
    Last modified:October 1, 2000 - v1
    Checksum:i52F936ACCB4FBA84
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE003852 Genomic DNA. Translation: AAF95184.1.
    PIRiF82125.
    RefSeqiNP_231670.1. NC_002505.1.
    WP_001263690.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF95184; AAF95184; VC_2036.
    GeneIDi2613415.
    KEGGivch:VC2036.
    PATRICi20083100. VBIVibCho83274_1944.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE003852 Genomic DNA. Translation: AAF95184.1.
    PIRiF82125.
    RefSeqiNP_231670.1. NC_002505.1.
    WP_001263690.1. NC_002505.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MB4X-ray1.84A/B1-370[»]
    1MC4X-ray2.77A1-370[»]
    3PZRX-ray1.75A/B1-370[»]
    3Q0EX-ray1.80A/B1-370[»]
    4R5MX-ray1.89A/B1-370[»]
    ProteinModelPortaliQ9KQG2.
    SMRiQ9KQG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243277.VC2036.

    Proteomic databases

    PRIDEiQ9KQG2.

    Protocols and materials databases

    DNASUi2613415.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAF95184; AAF95184; VC_2036.
    GeneIDi2613415.
    KEGGivch:VC2036.
    PATRICi20083100. VBIVibCho83274_1944.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.
    BioCyciMetaCyc:MONOMER-15807.
    VCHO:VC2036-MONOMER.
    BRENDAi1.2.1.11. 6626.

    Miscellaneous databases

    EvolutionaryTraceiQ9KQG2.

    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 nameiDHAS1_VIBCH
    AccessioniPrimary (citable) accession number: Q9KQG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: October 1, 2000
    Last modified: November 2, 2016
    This is version 99 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. 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.