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Protein

Aspartate-semialdehyde dehydrogenase 2

Gene

asd2

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

Kineticsi

  1. KM=0.16 mM for L-aspartate 4-semialdehyde1 Publication
  2. KM=0.36 mM for NADP+1 Publication
  3. KM=22 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 sitei101 – 1011PhosphateUniRule annotation
    Active sitei132 – 1321Acyl-thioester intermediate1 Publication
    Binding sitei159 – 1591SubstrateUniRule annotation
    Binding sitei216 – 2161PhosphateUniRule annotation
    Binding sitei238 – 2381SubstrateUniRule annotation
    Active sitei245 – 2451Proton acceptorUniRule annotation
    Binding sitei316 – 3161NADPUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 164NADPUniRule annotation
    Nucleotide bindingi41 – 422NADPUniRule annotation
    Nucleotide bindingi162 – 1632NADPUniRule annotation

    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

    BRENDAi1.2.1.11. 6626.
    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate-semialdehyde dehydrogenase 2 (EC:1.2.1.111 Publication)
    Short name:
    ASA dehydrogenase 2
    Short name:
    ASADH 2
    Alternative name(s):
    Aspartate-beta-semialdehyde dehydrogenase 2
    Gene namesi
    Name:asd2
    Synonyms:asd
    Ordered Locus Names:VC_2107
    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 – 337337Aspartate-semialdehyde dehydrogenase 2PRO_0000141394Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi243277.VC2107.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117Combined sources
    Helixi15 – 2612Combined sources
    Beta strandi31 – 388Combined sources
    Turni40 – 445Combined sources
    Beta strandi46 – 494Combined sources
    Beta strandi52 – 587Combined sources
    Helixi59 – 613Combined sources
    Helixi64 – 663Combined sources
    Beta strandi68 – 725Combined sources
    Helixi76 – 8813Combined sources
    Beta strandi92 – 954Combined sources
    Turni99 – 1024Combined sources
    Turni111 – 1133Combined sources
    Helixi115 – 1239Combined sources
    Beta strandi125 – 1284Combined sources
    Helixi132 – 14817Combined sources
    Beta strandi150 – 16314Combined sources
    Helixi165 – 18016Combined sources
    Helixi188 – 1914Combined sources
    Helixi195 – 1984Combined sources
    Turni204 – 2063Combined sources
    Helixi212 – 22413Combined sources
    Beta strandi231 – 24111Combined sources
    Beta strandi243 – 25513Combined sources
    Helixi259 – 26810Combined sources
    Beta strandi272 – 2743Combined sources
    Helixi281 – 2833Combined sources
    Beta strandi289 – 2913Combined sources
    Beta strandi293 – 3019Combined sources
    Beta strandi304 – 31613Combined sources
    Helixi317 – 33620Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QZ9X-ray2.20A/B/C2-337[»]
    2R00X-ray2.03A/B/C2-337[»]
    ProteinModelPortaliP23247.
    SMRiP23247. Positions 2-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23247.

    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.
    OMAiKWHKGII.
    OrthoDBiEOG6JB158.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_02121. ASADH.
    InterProiIPR000319. Asp-semialdehyde_DH_CS.
    IPR012080. Asp_semialdehyde_DH.
    IPR005986. Asp_semialdehyde_DH_beta.
    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.
    TIGRFAMsiTIGR01296. asd_B. 1 hit.
    PROSITEiPS01103. ASD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23247-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQQFNVAIF GATGAVGETM LEVLQEREFP VDELFLLASE RSEGKTYRFN
    60 70 80 90 100
    GKTVRVQNVE EFDWSQVHIA LFSAGGELSA KWAPIAAEAG VVVIDNTSHF
    110 120 130 140 150
    RYDYDIPLVV PEVNPEAIAE FRNRNIIANP NCSTIQMLVA LKPIYDAVGI
    160 170 180 190 200
    ERINVTTYQS VSGAGKAGID ELAGQTAKLL NGYPAETNTF SQQIAFNCIP
    210 220 230 240 250
    QIDQFMDNGY TKEEMKMVWE TQKIFNDPSI MVNPTCVRVP VFYGHAEAVH
    260 270 280 290 300
    VETRAPIDAE QVMDMLEQTD GIELFRGADF PTQVRDAGGK DHVLVGRVRN
    310 320 330
    DISHHSGINL WVVADNVRKG AATNAVQIAE LLVRDYF
    Length:337
    Mass (Da):37,375
    Last modified:May 30, 2000 - v2
    Checksum:i143D7E55593308FD
    GO

    Sequence cautioni

    The sequence AAF95253.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1892NT → QA in CAA39048 (Ref. 1) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401E → D in strain: C7258.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X55363 Genomic DNA. Translation: CAA39048.1.
    Y15281 Genomic DNA. Translation: CAA75569.1.
    AE003852 Genomic DNA. Translation: AAF95253.1. Different initiation.
    PIRiB82118.
    S14523.
    RefSeqiNP_231739.1. NC_002505.1.
    WP_001886330.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF95253; AAF95253; VC_2107.
    GeneIDi2613363.
    KEGGivch:VC2107.
    PATRICi20083243. VBIVibCho83274_2013.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X55363 Genomic DNA. Translation: CAA39048.1.
    Y15281 Genomic DNA. Translation: CAA75569.1.
    AE003852 Genomic DNA. Translation: AAF95253.1. Different initiation.
    PIRiB82118.
    S14523.
    RefSeqiNP_231739.1. NC_002505.1.
    WP_001886330.1. NC_002505.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QZ9X-ray2.20A/B/C2-337[»]
    2R00X-ray2.03A/B/C2-337[»]
    ProteinModelPortaliP23247.
    SMRiP23247. Positions 2-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243277.VC2107.

    Protocols and materials databases

    DNASUi2613363.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAF95253; AAF95253; VC_2107.
    GeneIDi2613363.
    KEGGivch:VC2107.
    PATRICi20083243. VBIVibCho83274_2013.

    Phylogenomic databases

    eggNOGiENOG4105CM3. Bacteria.
    COG0136. LUCA.
    KOiK00133.
    OMAiKWHKGII.
    OrthoDBiEOG6JB158.

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00016.
    UPA00050; UER00463.
    UPA00051; UER00464.
    BRENDAi1.2.1.11. 6626.

    Miscellaneous databases

    EvolutionaryTraceiP23247.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_02121. ASADH.
    InterProiIPR000319. Asp-semialdehyde_DH_CS.
    IPR012080. Asp_semialdehyde_DH.
    IPR005986. Asp_semialdehyde_DH_beta.
    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.
    TIGRFAMsiTIGR01296. asd_B. 1 hit.
    PROSITEiPS01103. ASD. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Avest A.R., Frits R.M.
      Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CDV 101.
    2. Fando R., Benitez J.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: El Tor C7258 / Serotype O1.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.
    4. "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.
    5. "The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae."
      Viola R.E., Liu X., Ohren J.F., Faehnle C.R.
      Acta Crystallogr. D 64:321-330(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH L-ASPARTATE-SEMIALDEHYDE, SUBUNIT, DOMAIN.
      Strain: ATCC 39315 / El Tor Inaba N16961.

    Entry informationi

    Entry nameiDHAS2_VIBCH
    AccessioniPrimary (citable) accession number: P23247
    Secondary accession number(s): O34226, Q9KQ93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: May 30, 2000
    Last modified: January 20, 2016
    This is version 125 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.