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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei18 – 181Substrate; via carbonyl oxygen
    Binding sitei60 – 601Substrate
    Binding sitei85 – 851Substrate
    Binding sitei132 – 1321Substrate
    Active sitei162 – 1621Proton donor
    Metal bindingi162 – 1621ZincCurated
    Binding sitei243 – 2431Substrate; via carbonyl oxygen
    Active sitei249 – 2491Nucleophile
    Metal bindingi249 – 2491ZincCurated

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141E → Q: Abolishes enzyme activity. 1 Publication
    Mutagenesisi162 – 1621H → G or F: Abolishes enzyme activity. 2 Publications
    Mutagenesisi249 – 2491C → S: Abolishes enzyme activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 254254N(G),N(G)-dimethylarginine dimethylaminohydrolasePRO_0000398677Add
    BLAST

    Proteomic databases

    PaxDbiQ9I4E3.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi208964.PA1195.

    Structurei

    Secondary structure

    1
    254
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85Combined sources
    Helixi12 – 165Combined sources
    Beta strandi21 – 233Combined sources
    Helixi28 – 4215Combined sources
    Turni43 – 464Combined sources
    Beta strandi48 – 525Combined sources
    Turni59 – 624Combined sources
    Turni64 – 674Combined sources
    Beta strandi68 – 703Combined sources
    Beta strandi75 – 773Combined sources
    Helixi83 – 875Combined sources
    Helixi88 – 9912Combined sources
    Beta strandi104 – 1063Combined sources
    Helixi115 – 1173Combined sources
    Beta strandi118 – 1214Combined sources
    Beta strandi124 – 1296Combined sources
    Beta strandi131 – 1333Combined sources
    Helixi135 – 14713Combined sources
    Beta strandi151 – 1566Combined sources
    Beta strandi158 – 1625Combined sources
    Helixi163 – 1653Combined sources
    Beta strandi166 – 1694Combined sources
    Beta strandi174 – 1774Combined sources
    Helixi179 – 1813Combined sources
    Helixi185 – 1873Combined sources
    Beta strandi190 – 1945Combined sources
    Helixi197 – 2037Combined sources
    Beta strandi206 – 2083Combined sources
    Beta strandi211 – 2177Combined sources
    Helixi219 – 2268Combined sources
    Turni227 – 2293Combined sources
    Beta strandi231 – 2355Combined sources
    Helixi238 – 2414Combined sources
    Turni242 – 2443Combined sources
    Turni247 – 2504Combined sources
    Beta strandi252 – 2543Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9I4E3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 662Substrate binding

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H70X-ray1.80A1-254[»]
    3BPBX-ray2.81A/B1-254[»]
    3RHYX-ray2.18A/B1-254[»]
    ProteinModelPortaliQ9I4E3.
    SMRiQ9I4E3. Positions 1-254.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA1195.

    Proteomic databases

    PaxDbiQ9I4E3.

    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: September 7, 2016
    This is version 82 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.