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Protein

Agmatine deiminase

Gene

AIH

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the hydrolysis of agmatine into N-carbamoylputrescine in the arginine decarboxylase (ADC) pathway of putrescine biosynthesis, a basic polyamine.

Catalytic activityi

Agmatine + H2O = N-carbamoylputrescine + NH3.2 Publications

Enzyme regulationi

Inhibited by N-ethylmaleimide and iodoacetamide.1 Publication

Kineticsi

    1. Vmax=112 nmol/sec/mg enzyme with agmatine as substrate1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Pathwayi: putrescine biosynthesis via agmatine pathway

    This protein is involved in step 1 of the subpathway that synthesizes N-carbamoylputrescine from agmatine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Agmatine deiminase (AIH)
    This subpathway is part of the pathway putrescine biosynthesis via agmatine pathway, which is itself part of Amine and polyamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-carbamoylputrescine from agmatine, the pathway putrescine biosynthesis via agmatine pathway and in Amine and polyamine biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei366 – 3661Amidino-cysteine intermediateBy similarity

    GO - Molecular functioni

    • agmatine deiminase activity Source: TAIR
    • protein-arginine deiminase activity Source: InterPro

    GO - Biological processi

    • polyamine biosynthetic process Source: TAIR
    • putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Polyamine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-2641.
    UniPathwayiUPA00534; UER00285.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Agmatine deiminase (EC:3.5.3.12)
    Alternative name(s):
    Agmatine iminohydrolase
    Protein EMBRYO DEFECTIVE 1873
    Gene namesi
    Name:AIH
    Synonyms:EMB1873
    Ordered Locus Names:At5g08170
    ORF Names:T22D6.110
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G08170.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801C → A: Impairs enzyme activity but does not abolish it. 1 Publication
    Mutagenesisi229 – 2291C → A: No effect. 1 Publication
    Mutagenesisi230 – 2301C → A: No effect. 1 Publication
    Mutagenesisi366 – 3661C → A: Impairs enzyme activity but does not abolish it. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 383383Agmatine deiminasePRO_0000194350Add
    BLAST

    Proteomic databases

    PaxDbiQ8GWW7.
    PRIDEiQ8GWW7.

    PTM databases

    iPTMnetiQ8GWW7.

    Expressioni

    Gene expression databases

    GenevisibleiQ8GWW7. AT.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT5G08170.1.

    Structurei

    Secondary structure

    1
    383
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113Combined sources
    Beta strandi22 – 276Combined sources
    Turni33 – 353Combined sources
    Helixi38 – 403Combined sources
    Helixi41 – 5515Combined sources
    Beta strandi60 – 645Combined sources
    Helixi66 – 683Combined sources
    Helixi69 – 757Combined sources
    Beta strandi80 – 845Combined sources
    Helixi92 – 954Combined sources
    Beta strandi98 – 1014Combined sources
    Beta strandi114 – 1218Combined sources
    Turni124 – 1263Combined sources
    Helixi127 – 1304Combined sources
    Beta strandi132 – 1343Combined sources
    Helixi139 – 1413Combined sources
    Helixi142 – 1509Combined sources
    Beta strandi154 – 1607Combined sources
    Helixi163 – 1653Combined sources
    Beta strandi166 – 1683Combined sources
    Beta strandi170 – 1778Combined sources
    Helixi178 – 1814Combined sources
    Turni184 – 1863Combined sources
    Helixi192 – 20312Combined sources
    Beta strandi207 – 2126Combined sources
    Helixi219 – 2213Combined sources
    Helixi225 – 2273Combined sources
    Beta strandi229 – 2335Combined sources
    Beta strandi236 – 2416Combined sources
    Helixi249 – 26113Combined sources
    Beta strandi272 – 2776Combined sources
    Helixi286 – 2905Combined sources
    Beta strandi296 – 2983Combined sources
    Beta strandi315 – 3173Combined sources
    Beta strandi320 – 3245Combined sources
    Helixi331 – 34212Combined sources
    Beta strandi346 – 3516Combined sources
    Turni352 – 3543Combined sources
    Helixi355 – 3584Combined sources
    Turni359 – 3613Combined sources
    Helixi364 – 3674Combined sources
    Beta strandi368 – 3725Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VKPX-ray1.53A/B1-383[»]
    2Q3UX-ray1.53A/B1-383[»]
    3H7CX-ray1.50X2-383[»]
    3H7KX-ray1.84A2-383[»]
    ProteinModelPortaliQ8GWW7.
    SMRiQ8GWW7. Positions 2-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8GWW7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the agmatine deiminase family.Curated

    Phylogenomic databases

    eggNOGiENOG410IFVC. Eukaryota.
    COG2957. LUCA.
    HOGENOMiHOG000239346.
    InParanoidiQ8GWW7.
    KOiK10536.
    OMAiPLYMTDE.
    OrthoDBiEOG09360BUP.
    PhylomeDBiQ8GWW7.

    Family and domain databases

    HAMAPiMF_01841. Agmatine_deimin. 1 hit.
    InterProiIPR017754. Agmatine_deiminase.
    IPR007466. Peptidyl-Arg-deiminase_porph.
    [Graphical view]
    PfamiPF04371. PAD_porph. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03380. agmatine_aguA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8GWW7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEESRESPAE HGYYMPAEWD SHAQTWIGWP ERQDNWRHNA LPAQRVFADV
    60 70 80 90 100
    AKAISKFEPV TVCASPAQWE NARKQLPEDI RVVEMSMNDS WFRDSGPTFI
    110 120 130 140 150
    VRKRPVKLSS LNRNIAGIDW NFNAWGGAND GCYNDWSHDL LVSRKILALE
    160 170 180 190 200
    RIPRFQHSMI LEGGSIHVDG EGTCLVTEEC LLNKNRNPHM SKEQIEEELK
    210 220 230 240 250
    KYLGVQSFIW LPRGLYGDED TNGHIDNMCC FARPGVVLLS WTDDETDPQY
    260 270 280 290 300
    ERSVEALSVL SNSIDARGRK IQVIKLYIPE PLYMTEEESS GITQDGEAIP
    310 320 330 340 350
    RLAGTRLAAS YVNFYIANGG IIAPQFGDPI RDKEAIRVLS DTFPHHSVVG
    360 370 380
    IENAREIVLA GGNIHCITQQ QPAEPTSVAE NGH
    Length:383
    Mass (Da):43,155
    Last modified:August 16, 2005 - v2
    Checksum:iE8289ED058B2BFD7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491D → G in BAC43189 (PubMed:11910074).Curated
    Sequence conflicti49 – 491D → G in AAO63405 (PubMed:14593172).Curated
    Sequence conflicti59 – 591P → L in BAB59127 (Ref. 5) Curated
    Sequence conflicti126 – 1261G → V in BAB59127 (Ref. 5) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL357612 Genomic DNA. Translation: CAB93718.1.
    CP002688 Genomic DNA. Translation: AED91261.1.
    AK118589 mRNA. Translation: BAC43189.1.
    BT005341 mRNA. Translation: AAO63405.1.
    AB062682 mRNA. Translation: BAB59127.1.
    PIRiT50502.
    RefSeqiNP_196434.1. NM_120900.5.
    UniGeneiAt.25550.

    Genome annotation databases

    EnsemblPlantsiAT5G08170.1; AT5G08170.1; AT5G08170.
    GeneIDi830713.
    GrameneiAT5G08170.1; AT5G08170.1; AT5G08170.
    KEGGiath:AT5G08170.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL357612 Genomic DNA. Translation: CAB93718.1.
    CP002688 Genomic DNA. Translation: AED91261.1.
    AK118589 mRNA. Translation: BAC43189.1.
    BT005341 mRNA. Translation: AAO63405.1.
    AB062682 mRNA. Translation: BAB59127.1.
    PIRiT50502.
    RefSeqiNP_196434.1. NM_120900.5.
    UniGeneiAt.25550.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VKPX-ray1.53A/B1-383[»]
    2Q3UX-ray1.53A/B1-383[»]
    3H7CX-ray1.50X2-383[»]
    3H7KX-ray1.84A2-383[»]
    ProteinModelPortaliQ8GWW7.
    SMRiQ8GWW7. Positions 2-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT5G08170.1.

    PTM databases

    iPTMnetiQ8GWW7.

    Proteomic databases

    PaxDbiQ8GWW7.
    PRIDEiQ8GWW7.

    Protocols and materials databases

    DNASUi830713.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G08170.1; AT5G08170.1; AT5G08170.
    GeneIDi830713.
    GrameneiAT5G08170.1; AT5G08170.1; AT5G08170.
    KEGGiath:AT5G08170.

    Organism-specific databases

    TAIRiAT5G08170.

    Phylogenomic databases

    eggNOGiENOG410IFVC. Eukaryota.
    COG2957. LUCA.
    HOGENOMiHOG000239346.
    InParanoidiQ8GWW7.
    KOiK10536.
    OMAiPLYMTDE.
    OrthoDBiEOG09360BUP.
    PhylomeDBiQ8GWW7.

    Enzyme and pathway databases

    UniPathwayiUPA00534; UER00285.
    BioCyciMetaCyc:MONOMER-2641.

    Miscellaneous databases

    EvolutionaryTraceiQ8GWW7.
    PROiQ8GWW7.

    Gene expression databases

    GenevisibleiQ8GWW7. AT.

    Family and domain databases

    HAMAPiMF_01841. Agmatine_deimin. 1 hit.
    InterProiIPR017754. Agmatine_deiminase.
    IPR007466. Peptidyl-Arg-deiminase_porph.
    [Graphical view]
    PfamiPF04371. PAD_porph. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03380. agmatine_aguA. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAGUA_ARATH
    AccessioniPrimary (citable) accession number: Q8GWW7
    Secondary accession number(s): Q94IC7, Q9LEZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: August 16, 2005
    Last modified: September 7, 2016
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.