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Protein

N(G),N(G)-dimethylarginine dimethylaminohydrolase

Gene

PA1195

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS.

Catalytic activityi

N(omega),N(omega)-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline.2 Publications

Enzyme regulationi

Inhibited by zinc ions. Competitively inhibited by lysine.1 Publication

Kineticsi

  1. KM=44 µM for N-methyl-L-arginine1 Publication
  2. KM=39 µM for N,N-dimethyl-L-arginine1 Publication
  3. KM=26 µM for S-methyl-L-thiocitrulline1 Publication

    pH dependencei

    Optimum pH is 7-8.5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei18Substrate; via carbonyl oxygen1
    Binding sitei60Substrate1
    Binding sitei85Substrate1
    Binding sitei132Substrate1
    Active sitei162Proton donor1
    Metal bindingi162ZincCurated1
    Binding sitei243Substrate; via carbonyl oxygen1
    Active sitei249Nucleophile1
    Metal bindingi249ZincCurated1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.5.3.18. 5087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N(G),N(G)-dimethylarginine dimethylaminohydrolase (EC:3.5.3.18)
    Short name:
    DDAH
    Short name:
    Dimethylarginine dimethylaminohydrolase
    Alternative name(s):
    Dimethylargininase
    Gene namesi
    Ordered Locus Names:PA1195
    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

    PseudoCAPiPA1195.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi114E → Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi162H → G or F: Abolishes enzyme activity. 2 Publications1
    Mutagenesisi249C → S: Abolishes enzyme activity. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003986771 – 254N(G),N(G)-dimethylarginine dimethylaminohydrolaseAdd BLAST254

    Proteomic databases

    PaxDbiQ9I4E3.
    PRIDEiQ9I4E3.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi208964.PA1195.

    Structurei

    Secondary structure

    1254
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 8Combined sources5
    Helixi12 – 16Combined sources5
    Beta strandi21 – 23Combined sources3
    Helixi28 – 42Combined sources15
    Turni43 – 46Combined sources4
    Beta strandi48 – 52Combined sources5
    Turni59 – 62Combined sources4
    Turni64 – 67Combined sources4
    Beta strandi68 – 70Combined sources3
    Beta strandi75 – 77Combined sources3
    Helixi83 – 87Combined sources5
    Helixi88 – 99Combined sources12
    Beta strandi104 – 106Combined sources3
    Helixi115 – 117Combined sources3
    Beta strandi118 – 121Combined sources4
    Beta strandi124 – 129Combined sources6
    Beta strandi131 – 133Combined sources3
    Helixi135 – 147Combined sources13
    Beta strandi151 – 156Combined sources6
    Beta strandi158 – 162Combined sources5
    Helixi163 – 165Combined sources3
    Beta strandi166 – 169Combined sources4
    Beta strandi174 – 177Combined sources4
    Helixi179 – 181Combined sources3
    Helixi185 – 187Combined sources3
    Beta strandi190 – 194Combined sources5
    Helixi197 – 203Combined sources7
    Beta strandi206 – 208Combined sources3
    Beta strandi211 – 217Combined sources7
    Helixi219 – 226Combined sources8
    Turni227 – 229Combined sources3
    Beta strandi231 – 235Combined sources5
    Helixi238 – 241Combined sources4
    Turni242 – 244Combined sources3
    Turni247 – 250Combined sources4
    Beta strandi252 – 254Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1H70X-ray1.80A1-254[»]
    3BPBX-ray2.81A/B1-254[»]
    3RHYX-ray2.18A/B1-254[»]
    ProteinModelPortaliQ9I4E3.
    SMRiQ9I4E3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9I4E3.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni65 – 66Substrate binding2

    Sequence similaritiesi

    Belongs to the DDAH family.Curated

    Phylogenomic databases

    eggNOGiENOG4106V2I. Bacteria.
    COG1834. LUCA.
    HOGENOMiHOG000161035.
    InParanoidiQ9I4E3.
    KOiK01482.
    OMAiSCFVEDT.
    PhylomeDBiQ9I4E3.

    Family and domain databases

    InterProiIPR033199. DDAH/AD.
    [Graphical view]
    PANTHERiPTHR12737. PTHR12737. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9I4E3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFKHIIARTP ARSLVDGLTS SHLGKPDYAK ALEQHNAYIR ALQTCDVDIT
    60 70 80 90 100
    LLPPDERFPD SVFVEDPVLC TSRCAIITRP GAESRRGETE IIEETVQRFY
    110 120 130 140 150
    PGKVERIEAP GTVEAGDIMM VGDHFYIGES ARTNAEGARQ MIAILEKHGL
    160 170 180 190 200
    SGSVVRLEKV LHLKTGLAYL EHNNLLAAGE FVSKPEFQDF NIIEIPEEES
    210 220 230 240 250
    YAANCIWVNE RVIMPAGYPR TREKIARLGY RVIEVDTSEY RKIDGGVSCM

    SLRF
    Length:254
    Mass (Da):28,470
    Last modified:March 1, 2001 - v1
    Checksum:i28E9FC2F61E3EBE2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04584.1.
    PIRiF83497.
    RefSeqiNP_249886.1. NC_002516.2.
    WP_003086612.1. NZ_ASJY01000157.1.

    Genome annotation databases

    EnsemblBacteriaiAAG04584; AAG04584; PA1195.
    GeneIDi883112.
    KEGGipae:PA1195.
    PATRICi19836710. VBIPseAer58763_1241.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04584.1.
    PIRiF83497.
    RefSeqiNP_249886.1. NC_002516.2.
    WP_003086612.1. NZ_ASJY01000157.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1H70X-ray1.80A1-254[»]
    3BPBX-ray2.81A/B1-254[»]
    3RHYX-ray2.18A/B1-254[»]
    ProteinModelPortaliQ9I4E3.
    SMRiQ9I4E3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA1195.

    Proteomic databases

    PaxDbiQ9I4E3.
    PRIDEiQ9I4E3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG04584; AAG04584; PA1195.
    GeneIDi883112.
    KEGGipae:PA1195.
    PATRICi19836710. VBIPseAer58763_1241.

    Organism-specific databases

    PseudoCAPiPA1195.

    Phylogenomic databases

    eggNOGiENOG4106V2I. Bacteria.
    COG1834. LUCA.
    HOGENOMiHOG000161035.
    InParanoidiQ9I4E3.
    KOiK01482.
    OMAiSCFVEDT.
    PhylomeDBiQ9I4E3.

    Enzyme and pathway databases

    BRENDAi3.5.3.18. 5087.

    Miscellaneous databases

    EvolutionaryTraceiQ9I4E3.

    Family and domain databases

    InterProiIPR033199. DDAH/AD.
    [Graphical view]
    PANTHERiPTHR12737. PTHR12737. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDDAH_PSEAE
    AccessioniPrimary (citable) accession number: Q9I4E3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: March 1, 2001
    Last modified: November 2, 2016
    This is version 84 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.