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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. no protein annotated in this organism
    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. no protein annotated in this organism
    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. no protein annotated in this organism
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721NADP1 Publication
    Binding sitei101 – 1011PhosphateUniRule annotation
    Active sitei134 – 1341Acyl-thioester intermediate1 Publication
    Binding sitei161 – 1611Substrate1 Publication
    Binding sitei192 – 1921NADP; via carbonyl oxygen1 Publication
    Binding sitei240 – 2401Substrate1 Publication
    Binding sitei243 – 2431PhosphateUniRule annotation
    Binding sitei267 – 2671Substrate1 Publication
    Active sitei274 – 2741Proton acceptor1 Publication
    Binding sitei350 – 3501NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 124NADP1 Publication
    Nucleotide bindingi36 – 372NADP1 Publication
    Nucleotide bindingi164 – 1652NADP1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Aspartate-semialdehyde dehydrogenase 1PRO_0000411126Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei134 – 1341S-cysteinyl cysteine; in inhibited form

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi243277.VC2036.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76Combined sources
    Helixi11 – 2212Combined sources
    Helixi25 – 284Combined sources
    Beta strandi29 – 3810Combined sources
    Beta strandi40 – 423Combined sources
    Beta strandi46 – 483Combined sources
    Helixi59 – 624Combined sources
    Beta strandi66 – 705Combined sources
    Helixi74 – 8613Combined sources
    Beta strandi92 – 954Combined sources
    Turni99 – 1024Combined sources
    Beta strandi106 – 1094Combined sources
    Helixi111 – 12313Combined sources
    Beta strandi128 – 1314Combined sources
    Helixi134 – 14815Combined sources
    Beta strandi152 – 16110Combined sources
    Helixi163 – 1653Combined sources
    Helixi168 – 19023Combined sources
    Helixi196 – 20813Combined sources
    Turni215 – 2173Combined sources
    Beta strandi224 – 2274Combined sources
    Beta strandi234 – 2363Combined sources
    Helixi239 – 25113Combined sources
    Beta strandi255 – 2573Combined sources
    Beta strandi267 – 2693Combined sources
    Beta strandi271 – 28414Combined sources
    Helixi288 – 2969Combined sources
    Beta strandi300 – 3045Combined sources
    Helixi309 – 3157Combined sources
    Helixi318 – 3214Combined sources
    Beta strandi327 – 3359Combined sources
    Beta strandi338 – 34912Combined sources
    Turni350 – 3556Combined sources
    Helixi356 – 36914Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-369.
    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.
    OrthoDBiEOG67X1PS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_02121. ASADH.
    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
    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. Positions 1-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243277.VC2036.

    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.
    OrthoDBiEOG67X1PS.

    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.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.
    2. "Expression and purification of aspartate beta-semialdehyde dehydrogenase from infectious microorganisms."
      Moore R.A., Bocik W.E., Viola R.E.
      Protein Expr. Purif. 25:189-194(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
      Strain: ATCC 39315 / El Tor Inaba N16961.
    3. "A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae."
      Blanco J., Moore R.A., Kabaleeswaran V., Viola R.E.
      Protein Sci. 12:27-33(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH NADP AND CYSTEINE, ENZYME REGULATION, ACTIVE SITE, SUBUNIT.
      Strain: ATCC 39315 / El Tor Inaba N16961.

    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: January 20, 2016
    This is version 96 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.