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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. 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 sitei101PhosphateUniRule annotation1
    Active sitei132Acyl-thioester intermediate1 Publication1
    Binding sitei159SubstrateUniRule annotation1
    Binding sitei216PhosphateUniRule annotation1
    Binding sitei238SubstrateUniRule annotation1
    Active sitei245Proton acceptorUniRule annotation1
    Binding sitei316NADPUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi13 – 16NADPUniRule annotation4
    Nucleotide bindingi41 – 42NADPUniRule annotation2
    Nucleotide bindingi162 – 163NADPUniRule annotation2

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00001413941 – 337Aspartate-semialdehyde dehydrogenase 2Add BLAST337

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi243277.VC2107.

    Structurei

    Secondary structure

    1337
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 11Combined sources7
    Helixi15 – 26Combined sources12
    Beta strandi31 – 38Combined sources8
    Turni40 – 44Combined sources5
    Beta strandi46 – 49Combined sources4
    Beta strandi52 – 58Combined sources7
    Helixi59 – 61Combined sources3
    Helixi64 – 66Combined sources3
    Beta strandi68 – 72Combined sources5
    Helixi76 – 88Combined sources13
    Beta strandi92 – 95Combined sources4
    Turni99 – 102Combined sources4
    Turni111 – 113Combined sources3
    Helixi115 – 123Combined sources9
    Beta strandi125 – 128Combined sources4
    Helixi132 – 148Combined sources17
    Beta strandi150 – 163Combined sources14
    Helixi165 – 180Combined sources16
    Helixi188 – 191Combined sources4
    Helixi195 – 198Combined sources4
    Turni204 – 206Combined sources3
    Helixi212 – 224Combined sources13
    Beta strandi231 – 241Combined sources11
    Beta strandi243 – 255Combined sources13
    Helixi259 – 268Combined sources10
    Beta strandi272 – 274Combined sources3
    Helixi281 – 283Combined sources3
    Beta strandi289 – 291Combined sources3
    Beta strandi293 – 301Combined sources9
    Beta strandi304 – 316Combined sources13
    Helixi317 – 336Combined sources20

    3D structure databases

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

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_02121. ASADH. 1 hit.
    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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti188 – 189NT → QA in CAA39048 (Ref. 1) Curated2

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti40E → D in strain: C7258. 1

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2QZ9X-ray2.20A/B/C2-337[»]
    2R00X-ray2.03A/B/C2-337[»]
    ProteinModelPortaliP23247.
    SMRiP23247.
    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.

    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. 1 hit.
    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...

    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: November 30, 2016
    This is version 129 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.