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B2FLQ2

- B2FLQ2_STRMK

UniProt

B2FLQ2 - B2FLQ2_STRMK

Protein

Alanine racemase

Gene

Smlt0568

Organism
Stenotrophomonas maltophilia (strain K279a)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (10 Jun 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 annotationSAAS annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei33 – 331Proton acceptor; specific for D-alanineUniRule annotation
    Binding sitei129 – 1291SubstrateUniRule annotation
    Active sitei253 – 2531Proton acceptor; specific for L-alanineUniRule annotation
    Binding sitei301 – 3011Substrate; 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

    BioCyciSMAL522373:GJE8-550-MONOMER.
    UniPathwayiUPA00042; UER00497.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation)
    Gene namesi
    Ordered Locus Names:Smlt0568Imported
    OrganismiStenotrophomonas maltophilia (strain K279a)Imported
    Taxonomic identifieri522373 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
    ProteomesiUP000008840: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei33 – 331N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi522373.Smlt0568.

    Structurei

    3D structure databases

    ProteinModelPortaliB2FLQ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alanine racemase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0787.
    HOGENOMiHOG000031446.
    KOiK01775.
    OMAiLWQLEAI.
    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.
    IPR020622. Ala_racemase_pyridoxalP-BS.
    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.
    PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B2FLQ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPARALIDL GALRSNYRLA RELGGGKALA IIKADAYGHG AVRCAQALEG    50
    EADGFGVATI EEALELRQAG IRAPILLLEG IFELSDMALV AEHDFWFAVG 100
    SPWQLEAVAA FDSPRPLTVW LKLDSGMHRL GLDVDSFRAA HARLSALPEV 150
    ERIVLMTHLA RADELDSERT HEQAATFARA IDGLHGETSV CNSPALLGWP 200
    DVRSDWVRPG LMLYGANPLP DDNTLTERLR PVMTMQSKVI AERWIEAGEP 250
    VGYGARFVAK ARTRVGVVAL GYADGYPQFA PNGTPVLIDG QPGALIGRVS 300
    MDMLTVDLTA HPQAAVGSVV ELWGSAPTLA ELAPRCGVSA YQLPCAVKRV 350
    AKVYV 355
    Length:355
    Mass (Da):38,190
    Last modified:June 10, 2008 - v1
    Checksum:i176ACD33D4A8101A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM743169 Genomic DNA. Translation: CAQ44156.1.
    RefSeqiYP_001970470.1. NC_010943.1.

    Genome annotation databases

    EnsemblBacteriaiCAQ44156; CAQ44156; Smlt0568.
    GeneIDi6394528.
    KEGGisml:Smlt0568.
    PATRICi23696855. VBISteMal45202_0536.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM743169 Genomic DNA. Translation: CAQ44156.1 .
    RefSeqi YP_001970470.1. NC_010943.1.

    3D structure databases

    ProteinModelPortali B2FLQ2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 522373.Smlt0568.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAQ44156 ; CAQ44156 ; Smlt0568 .
    GeneIDi 6394528.
    KEGGi sml:Smlt0568.
    PATRICi 23696855. VBISteMal45202_0536.

    Phylogenomic databases

    eggNOGi COG0787.
    HOGENOMi HOG000031446.
    KOi K01775.
    OMAi LWQLEAI.
    OrthoDBi EOG6PP9NJ.

    Enzyme and pathway databases

    UniPathwayi UPA00042 ; UER00497 .
    BioCyci SMAL522373:GJE8-550-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.
    IPR020622. Ala_racemase_pyridoxalP-BS.
    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.
    PROSITEi PS00395. ALANINE_RACEMASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
      Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
      , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
      Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K279aImported.

    Entry informationi

    Entry nameiB2FLQ2_STRMK
    AccessioniPrimary (citable) accession number: B2FLQ2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 51 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