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Q31DD8

- SPEA_PROM9

UniProt

Q31DD8 - SPEA_PROM9

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Prochlorococcus marinus (strain MIT 9312)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

    Catalytic activityi

    L-arginine = agmatine + CO2.UniRule annotation

    Cofactori

    Magnesium.UniRule annotation
    Pyridoxal phosphate.UniRule 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

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciPMAR74546:GHRG-46-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:PMT9312_0046
    OrganismiProchlorococcus marinus (strain MIT 9312)
    Taxonomic identifieri74546 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000002715: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 648648Biosynthetic arginine decarboxylasePRO_1000024261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei109 – 1091N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi74546.PMT9312_0046.

    Structurei

    3D structure databases

    ProteinModelPortaliQ31DD8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni291 – 30111Substrate-bindingUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1166.
    HOGENOMiHOG000029191.
    KOiK01585.
    OMAiIDHYVDG.
    OrthoDBiEOG676Z0R.

    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.
    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.
    TIGRFAMsiTIGR01273. speA. 1 hit.
    PROSITEiPS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q31DD8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTNFEPKKLK NIWTIEDSIS TYNIDKWGDK YFSINSKGNI SVTKDIKSEN    50
    KIDLFKLVKE LKSREINPPL IIRFNDILKD RINALHDSFF KAIKTYKYKN 100
    IYQGVFPVKC NQQKNVLEKI IEFGSQWNFG LEVGSKSELL IGLALLENQN 150
    SLLICNGYKD KKYIEIATLA RKLGKNPIIV IEQRDEVKRI IQAVQELNAT 200
    PLIGIRAKLS SKSSGRWGKS IGDNSKFGLS IPEIMLTIKE LKEANLINEM 250
    KLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LCKLGAPMQY IDVGGGLGID 300
    FDGTKTSSNT STNYSLQNYA NDVIATIKDS CELNNIKHPI IISESGRAII 350
    SHCSVLIFNV LGTSHVSSKL QIFDKKNQQL IISNLLETFY ELKKLKNKKI 400
    NLSQIIELWN DAKKFKEDCL VAFRLGFLSL AERAYAEELT WACAKEISKN 450
    LNNDAINHPD LSEITETLAS TYYANLSIFK SIPDSWAINQ IFPIVPIHRH 500
    LEEPFCKGNF ADLTCDSDGK LNNFIDDGKI KSLLNLHKPE EDKDYLIGIF 550
    MTGAYQEALG NLHNLFGSTN VVHIDINQDN SYKVKNIIKE DSKSEILQLL 600
    DYSSASLVES IRINTESAID QKKLTIEEAR KLMDQIEISL RKSSYLSE 648
    Length:648
    Mass (Da):73,366
    Last modified:December 6, 2005 - v1
    Checksum:i7F89743E16C3B08A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000111 Genomic DNA. Translation: ABB49107.1.
    RefSeqiYP_396543.1. NC_007577.1.

    Genome annotation databases

    EnsemblBacteriaiABB49107; ABB49107; PMT9312_0046.
    GeneIDi3764827.
    KEGGipmi:PMT9312_0046.
    PATRICi23003698. VBIProMar70153_0046.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000111 Genomic DNA. Translation: ABB49107.1 .
    RefSeqi YP_396543.1. NC_007577.1.

    3D structure databases

    ProteinModelPortali Q31DD8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 74546.PMT9312_0046.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB49107 ; ABB49107 ; PMT9312_0046 .
    GeneIDi 3764827.
    KEGGi pmi:PMT9312_0046.
    PATRICi 23003698. VBIProMar70153_0046.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci PMAR74546:GHRG-46-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.
    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.
    TIGRFAMsi TIGR01273. speA. 1 hit.
    PROSITEi PS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MIT 9312.

    Entry informationi

    Entry nameiSPEA_PROM9
    AccessioniPrimary (citable) accession number: Q31DD8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 59 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

    Complete proteome

    Documents

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

    External Data

    Dasty 3