Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5SHU0

- Q5SHU0_THET8

UniProt

Q5SHU0 - Q5SHU0_THET8

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

    Catalytic activityi

    L-arginine = agmatine + CO2.UniRule annotationSAAS annotation

    Cofactori

    Magnesium.UniRule annotationSAAS annotation
    Pyridoxal phosphate.UniRule annotationSAAS annotation

    Pathwayi

    GO - Molecular functioni

    1. arginine decarboxylase activity Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine catabolic process Source: InterPro
    2. spermidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    DecarboxylaseUniRule annotationSAAS annotation, Lyase

    Keywords - Biological processi

    Polyamine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotation, Pyridoxal phosphateUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-1679-MONOMER.
    UniPathwayiUPA00186; UER00284.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
    Short name:
    ADCUniRule annotation
    Gene namesi
    Name:speAUniRule annotation
    Ordered Locus Names:TTHA1640Imported
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)Imported
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi300852.TTHA1640.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5SHU0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1166.
    HOGENOMiHOG000029191.
    KOiK01585.
    OMAiIDHYVDG.
    OrthoDBiEOG676Z0R.
    PhylomeDBiQ5SHU0.

    Family and domain databases

    Gene3Di2.40.37.10. 2 hits.
    3.20.20.10. 1 hit.
    HAMAPiMF_01417. SpeA.
    InterProiIPR009006. Ala_racemase/Decarboxylase_C.
    IPR002985. Arg_decrbxlase.
    IPR022643. De-COase2_C.
    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.
    TIGRFAMsiTIGR01273. speA. 1 hit.
    PROSITEiPS00878. ODR_DC_2_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5SHU0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKRFTLKDA EELYLVPHWS GGFFRVGEKG DLEVTPLGPK GPAASLLEIV    50
    EALRDEGRPL PLVLRFPQIL EARVRDLNEA FLEAMAKYGY QGTYRGVYPV 100
    KVNQRRLVLE TVARAGRPYH LGLEAGSKPE LALILAQDLS EEALITTNGF 150
    KDDDFVRLAL MGRKLGRNVV ITLEKFAELF RVLRLSKELG VKPLLGIRYK 200
    LKAKGAGQWE ASGGENAKFG LTTPEIVRAV EVLQEEGLLD ALVMLHAHIG 250
    SQVTDIRRIK AAVREAAQTY VQLRKLGAPL RYLNLGGGLA VDYDGSKTNF 300
    YASANYTLSE YAENLVYVTK EVVEAQGEPH PILVTESGRA ITAYHEVLVL 350
    QVIDVIAPPG EARPSPPPPE AHPLVKELWE SLQSLSPKNF QEVYHDAFAD 400
    KETLQTLYDL GLVSLRDRAL AEEIFYHIAR RVQTIAQNLP YVPDELEDLE 450
    KLLADKLVCN FSVFQSLPDA WAIHQLFPVV PLSRLLEPPT RRATLVDISC 500
    DSDGKMDRFI DLHDVRQTLP VHPVRPGEPY YLGVFLVGAY QDVLGSNHNL 550
    FGQVGEAHVR VEEEGFAIER FVGGETAERV IEKMGFTARE LMLGVERLVR 600
    QSRLSPVEKG AFLERYAREL QGYTYLED 628
    Length:628
    Mass (Da):70,241
    Last modified:December 21, 2004 - v1
    Checksum:i565F8577FDF8D999
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD71463.1.
    RefSeqiWP_011228825.1. NC_006461.1.
    YP_144906.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD71463; BAD71463; BAD71463.
    GeneIDi3169310.
    KEGGittj:TTHA1640.
    PATRICi23958235. VBITheThe93045_1610.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD71463.1 .
    RefSeqi WP_011228825.1. NC_006461.1.
    YP_144906.1. NC_006461.1.

    3D structure databases

    ProteinModelPortali Q5SHU0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA1640.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD71463 ; BAD71463 ; BAD71463 .
    GeneIDi 3169310.
    KEGGi ttj:TTHA1640.
    PATRICi 23958235. VBITheThe93045_1610.

    Phylogenomic databases

    eggNOGi COG1166.
    HOGENOMi HOG000029191.
    KOi K01585.
    OMAi IDHYVDG.
    OrthoDBi EOG676Z0R.
    PhylomeDBi Q5SHU0.

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci TTHE300852:GH8R-1679-MONOMER.

    Family and domain databases

    Gene3Di 2.40.37.10. 2 hits.
    3.20.20.10. 1 hit.
    HAMAPi MF_01417. SpeA.
    InterProi IPR009006. Ala_racemase/Decarboxylase_C.
    IPR002985. Arg_decrbxlase.
    IPR022643. De-COase2_C.
    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.
    TIGRFAMsi TIGR01273. speA. 1 hit.
    PROSITEi PS00878. ODR_DC_2_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579Imported.

    Entry informationi

    Entry nameiQ5SHU0_THET8
    AccessioniPrimary (citable) accession number: Q5SHU0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: December 21, 2004
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3