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Q7TUJ9

- SPEA_PROMM

UniProt

Q7TUJ9 - SPEA_PROMM

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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

    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

    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:PMT_2150
    OrganismiProchlorococcus marinus (strain MIT 9313)
    Taxonomic identifieri74547 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001423: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 648648Biosynthetic arginine decarboxylasePRO_0000149969Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Protein-protein interaction databases

    STRINGi74547.PMT2150.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TUJ9.
    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.
    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.

    Q7TUJ9-1 [UniParc]FASTAAdd to Basket

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    MSAADPIQDN KSWTVADSAA LYGLDHWGHP YFSANANGHV QVQPRGDQGS    50
    CLDLVELVEE LKSRNLNLPL LIRFDDILED RLERLHSAFE EAISKYGYAG 100
    RYQGVFPVKC NQQRHVVEQL VESGRQWHFG LEAGSKAELL IALSLVNDPE 150
    ALLICNGYKD QRYIETAILA RRLGRQPVVV IEQPDEVERI IRSSQELGAA 200
    PFLGVRAKLT TRSTGHWSSS VGEKAKFGLS VPDLLATVEA LRQADLLSDL 250
    RLLHFHIGSQ INDIAVLKDA LQEAAQIYVE LTKLGAPMGY LDVGGGLGVD 300
    YDGSRSASAA STNYSLQNYA NDVVATVREC CKPHGITLPI LVSESGRAIA 350
    SHFSILVFDV LGTGTVPGAI PKQTVEEPLT IHNLRETLSG VMATQKGAVS 400
    EISRLQEAWN DAIKFKEDAL AAFRLGYISL PERALAEQLT GACAEAIMGQ 450
    LPCNETIPDD LQSLRAVLAS TYYANLSIFR SAPDTWAIEQ LFPLMPIHRL 500
    NEEPTQLGHF ADLTCDSDGK LDRFIGNGQT KTLLELHNLR QNEAYMIGMF 550
    LAGAYQEVMG NLHNLFGSTN AVHIRLTTAG GYQVDHVVRG NTNSEVLEAM 600
    EHNPELLLER LRLASELAIQ RGELKINDVR RLMDHLEASL RQTTYLQG 648
    Length:648
    Mass (Da):71,364
    Last modified:October 1, 2003 - v1
    Checksum:iBBFEE45E4F8E395B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548175 Genomic DNA. Translation: CAE22324.1.
    RefSeqiNP_895974.1. NC_005071.1.

    Genome annotation databases

    EnsemblBacteriaiCAE22324; CAE22324; PMT_2150.
    GeneIDi1727896.
    KEGGipmt:PMT2150.
    PATRICi23013213. VBIProMar135351_2729.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548175 Genomic DNA. Translation: CAE22324.1 .
    RefSeqi NP_895974.1. NC_005071.1.

    3D structure databases

    ProteinModelPortali Q7TUJ9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 74547.PMT2150.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE22324 ; CAE22324 ; PMT_2150 .
    GeneIDi 1727896.
    KEGGi pmt:PMT2150.
    PATRICi 23013213. VBIProMar135351_2729.

    Phylogenomic databases

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

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MIT 9313.

    Entry informationi

    Entry nameiSPEA_PROMM
    AccessioniPrimary (citable) accession number: Q7TUJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 68 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3