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P22220

- SPE1_AVESA

UniProt

P22220 - SPE1_AVESA

Protein

Arginine decarboxylase

Gene

SPE1

Organism
Avena sativa (Oat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-arginine = agmatine + CO2.

    Cofactori

    Pyridoxal phosphate.
    Magnesium.

    Pathwayi

    GO - Molecular functioni

    1. arginine decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arginine catabolic process Source: InterPro
    2. putrescine biosynthetic process Source: UniProtKB-KW
    3. spermidine biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Putrescine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Magnesium, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14981.
    UniPathwayiUPA00186; UER00284.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine decarboxylase (EC:4.1.1.19)
    Short name:
    ADC
    Short name:
    ARGDC
    Gene namesi
    Name:SPE1
    OrganismiAvena sativa (Oat)
    Taxonomic identifieri4498 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaePoeaeAveninaeAvena

    Organism-specific databases

    GrameneiP22220.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 607607Arginine decarboxylasePRO_0000149948Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PRIDEiP22220.

    Structurei

    3D structure databases

    ProteinModelPortaliP22220.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 30011Substrate-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Family and domain databases

    Gene3Di2.40.37.10. 2 hits.
    3.20.20.10. 1 hit.
    InterProiIPR009006. Ala_racemase/Decarboxylase_C.
    IPR002985. Arg_decrbxlase.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view]
    PfamiPF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
    PRINTSiPR01180. ARGDCRBXLASE.
    PR01179. ODADCRBXLASE.
    SUPFAMiSSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    PROSITEiPS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22220-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKNYGDVYH VEGWGEPYFA VNKDGHLCVR IYGRETLPGQ EIDVLSVIEQ    50
    ATSADGTGKK LQFPMILRFP DVLRHRINSL HTAFANAIKY TQYGSVYQGV 100
    FPVKVNQHKD VVQDMVHFGY DHSYGLEAGS KPELLIAMSC LTKAKPGAYL 150
    VCNGYKDSAY VALALAARAM GLNVIIVLEM EEELDIVIEE SSKLGVEPVI 200
    GVRAKLLTKI PGHFGSTAGK HGKFGLPAEK IYEVAKKLKA LNKLHWLKLL 250
    HFHVGSMIPT TDIVFKAASE ASDIYCALVK EYGVETMTTL DCGGGLGVDY 300
    DGTRSGSSDM SVAYGLEEYA SSIVQAVRLK CDYHGVPHPV LCTESGRAMA 350
    SYHSMIILEA LSAIPEPKDD EDEATTEQLH GRIRDLSSKL QPTGLSMSSH 400
    AVHIKKHGIE MYKLGKKLSK SVTTDAHTIY NYHMNLSVFS LMPDYWGIQH 450
    LFPMMPVSRL DEKPTHKATL VDVTCDSDGK VDKFIRDTET MPLHPLDPKL 500
    GGYYVAVLLT GAYQEALSNK HNLFGGPSLV RVVGTGNGGA FNVEAALLGS 550
    TTEELIGTVS YDVKQDISSV IEERARENKV WEMVEKLVES GLHTMPYLAD 600
    YKPPPMA 607
    Length:607
    Mass (Da):66,706
    Last modified:August 1, 1991 - v1
    Checksum:i757114B2C02EF8A5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56802 mRNA. Translation: CAA40137.1.
    PIRiS12265.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56802 mRNA. Translation: CAA40137.1 .
    PIRi S12265.

    3D structure databases

    ProteinModelPortali P22220.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P22220.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P22220.

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci MetaCyc:MONOMER-14981.

    Family and domain databases

    Gene3Di 2.40.37.10. 2 hits.
    3.20.20.10. 1 hit.
    InterProi IPR009006. Ala_racemase/Decarboxylase_C.
    IPR002985. Arg_decrbxlase.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view ]
    Pfami PF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001336. Arg_decrbxlase. 1 hit.
    PRINTSi PR01180. ARGDCRBXLASE.
    PR01179. ODADCRBXLASE.
    SUPFAMi SSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    PROSITEi PS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing."
      Bell E., Malmberg R.L.
      Mol. Gen. Genet. 224:431-436(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 427-437.
      Tissue: Leaf.

    Entry informationi

    Entry nameiSPE1_AVESA
    AccessioniPrimary (citable) accession number: P22220
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3