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B2TKD2

- B2TKD2_CLOBB

UniProt

B2TKD2 - B2TKD2_CLOBB

Protein

Alanine racemase

Gene

alr

Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 Jul 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.UniRule annotation

    Catalytic activityi

    L-alanine = D-alanine.UniRule annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei38 – 381Proton acceptor; specific for D-alanineUniRule annotation
    Binding sitei136 – 1361SubstrateUniRule annotation
    Active sitei267 – 2671Proton acceptor; specific for L-alanineUniRule annotation
    Binding sitei315 – 3151Substrate; via amide nitrogenUniRule annotation

    GO - Molecular functioni

    1. alanine racemase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. D-alanine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    IsomeraseUniRule annotationSAAS annotationImported

    Keywords - Ligandi

    Pyridoxal phosphateUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciCBOT508765:GJ4H-1564-MONOMER.
    UniPathwayiUPA00042; UER00497.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation)
    Gene namesi
    Name:alrImported
    Ordered Locus Names:CLL_A1573Imported
    ORF Names:CB17B1496Imported
    OrganismiClostridium botulinum (strain Eklund 17B / Type B)Imported
    Taxonomic identifieri935198 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001195: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi508765.CLL_A1573.

    Structurei

    3D structure databases

    ProteinModelPortaliB2TKD2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alanine racemase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0787.
    HOGENOMiHOG000031444.
    KOiK01775.
    OMAiWRDMARR.
    OrthoDBiEOG6PP9NJ.

    Family and domain databases

    Gene3Di2.40.37.10. 1 hit.
    3.20.20.10. 1 hit.
    HAMAPiMF_01201. Ala_racemase.
    InterProiIPR000821. Ala_racemase.
    IPR009006. Ala_racemase/Decarboxylase_C.
    IPR011079. Ala_racemase_C.
    IPR001608. Ala_racemase_N.
    IPR029066. PLP-binding_barrel.
    [Graphical view]
    PfamiPF00842. Ala_racemase_C. 1 hit.
    PF01168. Ala_racemase_N. 1 hit.
    [Graphical view]
    PRINTSiPR00992. ALARACEMASE.
    SMARTiSM01005. Ala_racemase_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    TIGRFAMsiTIGR00492. alr. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    B2TKD2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKIMRPVWA EIDLDAIAYN MRNIKKLAQN KDVIAVVKAD CYGHGALDVV    50
    PTLLENGASR LAVAVLTEAI ELRNNNITAP IMILGYTPEY LFEEVVNYDI 100
    EQTVYDLEYA KKLSHLAIKF NKKAKVHIAI DTGMGRIGFI PNEKAIKDIK 150
    KIYNLKGLDV IGIFTHFSTS DETDKEYTNE QFNKFTSFID MLSKVGVKIP 200
    IKHISNSGAI IDMPKTYLDS VRAGIILYGY YPSDEINKDN IKLKPALTLK 250
    ASLTRVQELD INSYISYGKT FKTERKSIIA TLPIGYADGY SRLLAPGAKV 300
    IINGKFSPII GRICMDQCMI DVTDIDDIHV GDEVIILGED GNLKLTANDL 350
    AKSMGTINYE ILCMLKYRIP RVYMKNGKIF TVRNYL 386
    Length:386
    Mass (Da):43,373
    Last modified:July 1, 2008 - v1
    Checksum:i1B36636BDEEB26D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001056 Genomic DNA. Translation: ACD22809.1.
    FR745875 Genomic DNA. Translation: CDH90485.1.
    RefSeqiWP_012423654.1. NC_010674.1.
    YP_001885767.1. NC_010674.1.

    Genome annotation databases

    EnsemblBacteriaiACD22809; ACD22809; CLL_A1573.
    GeneIDi6294126.
    KEGGicbk:CLL_A1573.
    PATRICi19395990. VBICloBot123574_1505.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001056 Genomic DNA. Translation: ACD22809.1 .
    FR745875 Genomic DNA. Translation: CDH90485.1 .
    RefSeqi WP_012423654.1. NC_010674.1.
    YP_001885767.1. NC_010674.1.

    3D structure databases

    ProteinModelPortali B2TKD2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 508765.CLL_A1573.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD22809 ; ACD22809 ; CLL_A1573 .
    GeneIDi 6294126.
    KEGGi cbk:CLL_A1573.
    PATRICi 19395990. VBICloBot123574_1505.

    Phylogenomic databases

    eggNOGi COG0787.
    HOGENOMi HOG000031444.
    KOi K01775.
    OMAi WRDMARR.
    OrthoDBi EOG6PP9NJ.

    Enzyme and pathway databases

    UniPathwayi UPA00042 ; UER00497 .
    BioCyci CBOT508765:GJ4H-1564-MONOMER.

    Family and domain databases

    Gene3Di 2.40.37.10. 1 hit.
    3.20.20.10. 1 hit.
    HAMAPi MF_01201. Ala_racemase.
    InterProi IPR000821. Ala_racemase.
    IPR009006. Ala_racemase/Decarboxylase_C.
    IPR011079. Ala_racemase_C.
    IPR001608. Ala_racemase_N.
    IPR029066. PLP-binding_barrel.
    [Graphical view ]
    Pfami PF00842. Ala_racemase_C. 1 hit.
    PF01168. Ala_racemase_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00992. ALARACEMASE.
    SMARTi SM01005. Ala_racemase_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    TIGRFAMsi TIGR00492. alr. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Clostridium botulinum strain Eklund."
      Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
      Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Eklund 17B / Type BImported.
    2. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: Eklund 17BImported.
    3. Shrivastava S., Brinkac L.M., Dodson R.J., Harkins D.M., Durkin A.S., Sutton G.
      Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: Eklund 17BImported.
    4. "Genomic and physiological variability within Group II (non-proteolytic) Clostridium botulinum."
      Stringer S.C., Carter A.T., Webb M.D., Wachnicka E., Crossman L.C., Sebaihia M., Peck M.W.
      BMC Genomics 14:333-333(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: B str. Eklund 17BImported.

    Entry informationi

    Entry nameiB2TKD2_CLOBB
    AccessioniPrimary (citable) accession number: B2TKD2
    Secondary accession number(s): U4PFB0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 1, 2008
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 56 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