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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)DescriptionActionsGraphical viewLength
    Active sitei366Amidino-cysteine intermediateBy similarity1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi180C → A: Impairs enzyme activity but does not abolish it. 1 Publication1
    Mutagenesisi229C → A: No effect. 1 Publication1
    Mutagenesisi230C → A: No effect. 1 Publication1
    Mutagenesisi366C → A: Impairs enzyme activity but does not abolish it. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001943501 – 383Agmatine deiminaseAdd BLAST383

    Proteomic databases

    PaxDbiQ8GWW7.

    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

    1383
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi9 – 11Combined sources3
    Beta strandi22 – 27Combined sources6
    Turni33 – 35Combined sources3
    Helixi38 – 40Combined sources3
    Helixi41 – 55Combined sources15
    Beta strandi60 – 64Combined sources5
    Helixi66 – 68Combined sources3
    Helixi69 – 75Combined sources7
    Beta strandi80 – 84Combined sources5
    Helixi92 – 95Combined sources4
    Beta strandi98 – 101Combined sources4
    Beta strandi114 – 121Combined sources8
    Turni124 – 126Combined sources3
    Helixi127 – 130Combined sources4
    Beta strandi132 – 134Combined sources3
    Helixi139 – 141Combined sources3
    Helixi142 – 150Combined sources9
    Beta strandi154 – 160Combined sources7
    Helixi163 – 165Combined sources3
    Beta strandi166 – 168Combined sources3
    Beta strandi170 – 177Combined sources8
    Helixi178 – 181Combined sources4
    Turni184 – 186Combined sources3
    Helixi192 – 203Combined sources12
    Beta strandi207 – 212Combined sources6
    Helixi219 – 221Combined sources3
    Helixi225 – 227Combined sources3
    Beta strandi229 – 233Combined sources5
    Beta strandi236 – 241Combined sources6
    Helixi249 – 261Combined sources13
    Beta strandi272 – 277Combined sources6
    Helixi286 – 290Combined sources5
    Beta strandi296 – 298Combined sources3
    Beta strandi315 – 317Combined sources3
    Beta strandi320 – 324Combined sources5
    Helixi331 – 342Combined sources12
    Beta strandi346 – 351Combined sources6
    Turni352 – 354Combined sources3
    Helixi355 – 358Combined sources4
    Turni359 – 361Combined sources3
    Helixi364 – 367Combined sources4
    Beta strandi368 – 372Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VKPX-ray1.53A/B1-383[»]
    2Q3UX-ray1.53A/B1-383[»]
    3H7CX-ray1.50X2-383[»]
    3H7KX-ray1.84A2-383[»]
    ProteinModelPortaliQ8GWW7.
    SMRiQ8GWW7.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti49D → G in BAC43189 (PubMed:11910074).Curated1
    Sequence conflicti49D → G in AAO63405 (PubMed:14593172).Curated1
    Sequence conflicti59P → L in BAB59127 (Ref. 5) Curated1
    Sequence conflicti126G → V in BAB59127 (Ref. 5) Curated1

    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_120900.6.
    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_120900.6.
    UniGeneiAt.25550.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi3702.AT5G08170.1.

    PTM databases

    iPTMnetiQ8GWW7.

    Proteomic databases

    PaxDbiQ8GWW7.

    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: November 30, 2016
    This is version 97 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.