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Q9KLD1

- SPEA_VIBCH

UniProt

Q9KLD1 - SPEA_VIBCH

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (29 Mar 2004)
      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: TIGR
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine catabolic process Source: InterPro
    2. polyamine biosynthetic process Source: TIGR
    3. 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:VC_A0815
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 640640Biosynthetic arginine decarboxylasePRO_0000149983Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi243277.VCA0815.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KLD1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 30011Substrate-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.
    IPR022644. De-COase2_N.
    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.
    SUPFAMiSSF51419. SSF51419. 1 hit.
    TIGRFAMsiTIGR01273. speA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9KLD1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRYDVEQPSK LDRVRADYNV HYWSQGFFGI DDQGEVYVSP RKDKAHQTQL    50
    SSIVKQLEAR DLNLPVLVRF PQILHQRVHN ICDAFNQAIE EYDYPNKYLL 100
    VYPIKVNQQK EVVDEILASQ AELEHKQLGL EAGSKPELLA VLAMAQQASS 150
    VIVCNGYKDR EYIRLALIGE KLGHKVFIVL EKLSELDLVL KEAKSLGVKP 200
    RLGLRIRLAS QGAGKWQSSG GEKSKFGLAA SQVLTVINRL KAENQLEALQ 250
    LVHFHLGSQM ANIRDVRNGV NEAVRFYCEL RELGAHIDFF DVGGGLAVDY 300
    DGTRSQSSNS MNYGLHEYAR NIVSTVSDVC NLYGQPRPVI ISESGRSITA 350
    HHAVLITNVI GTEAYSPEEI PAPGADAPML LKNMWRGFEE VQHGTDDRAL 400
    IEIYNDTQSD LSEAHSQFAT GVLNLEHRAW AEQLSLRIYH ELRQKMSNKN 450
    RFHRPILDEL QERLADKFFV NFSLFQSLPD AWGIDQVFPV LPLSGLEEMN 500
    DRRAVMLDIT CDSDGAVEQY VEGQGIESTL PVPAWTSDKP YLMGFFLVGA 550
    YQEILGDMHN LFGDTHSAVV NINDNGESEI AFINEGDTVE DMMRYVHIDV 600
    DKIRTNYRQL VSQRVAKEEQ ETVLAELELG LSGYTYLEDF 640
    Length:640
    Mass (Da):72,249
    Last modified:March 29, 2004 - v2
    Checksum:i851D1CE7D6E466F9
    GO

    Sequence cautioni

    The sequence AAF96713.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003853 Genomic DNA. Translation: AAF96713.1. Different initiation.
    PIRiE82414.
    RefSeqiNP_233201.1. NC_002506.1.

    Genome annotation databases

    EnsemblBacteriaiAAF96713; AAF96713; VC_A0815.
    GeneIDi2611850.
    KEGGivch:VCA0815.
    PATRICi20086176. VBIVibCho83274_3435.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003853 Genomic DNA. Translation: AAF96713.1 . Different initiation.
    PIRi E82414.
    RefSeqi NP_233201.1. NC_002506.1.

    3D structure databases

    ProteinModelPortali Q9KLD1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VCA0815.

    Protocols and materials databases

    DNASUi 2611850.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF96713 ; AAF96713 ; VC_A0815 .
    GeneIDi 2611850.
    KEGGi vch:VCA0815.
    PATRICi 20086176. VBIVibCho83274_3435.

    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.
    IPR022644. De-COase2_N.
    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 SSF51419. SSF51419. 1 hit.
    TIGRFAMsi TIGR01273. speA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.

    Entry informationi

    Entry nameiSPEA_VIBCH
    AccessioniPrimary (citable) accession number: Q9KLD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 29, 2004
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 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