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P0A6B5

- ALR1_SHIFL

UniProt

P0A6B5 - ALR1_SHIFL

Protein

Alanine racemase, biosynthetic

Gene

alr

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.1 Publication

    Catalytic activityi

    L-alanine = D-alanine.1 Publication

    Cofactori

    Pyridoxal phosphate.1 Publication

    pH dependencei

    Optimum pH is 8-10.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei34 – 341Proton acceptor; specific for D-alanineBy similarity
    Binding sitei129 – 1291SubstrateBy similarity
    Active sitei255 – 2551Proton acceptor; specific for L-alanineBy similarity
    Binding sitei303 – 3031Substrate; via amide nitrogenBy similarity

    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
    2. peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
    3. regulation of cell shape Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi5.1.1.1. 5712.
    UniPathwayiUPA00042; UER00497.
    UPA00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alanine racemase, biosynthetic (EC:5.1.1.1)
    Gene namesi
    Name:alr
    Ordered Locus Names:SF4152, S3578
    OrganismiShigella flexneri
    Taxonomic identifieri623 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Alanine racemase, biosyntheticPRO_0000114565Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP0A6B5.

    Interactioni

    Subunit structurei

    Monomer but homodimer in the presence of the substrate.1 Publication

    Protein-protein interaction databases

    STRINGi198214.SF4152.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A6B5.
    SMRiP0A6B5. Positions 1-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alanine racemase family.Curated

    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.

    P0A6B5-1 [UniParc]FASTAAdd to Basket

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    MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP    50
    DADAFGVARL EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH 100
    NEEQLAALEE ASLDEPVTVW MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV 150
    RQPVNIVSHF ARADEPKCGA TEKQLAIFNT FCEGKPGQRS IAASGGILLW 200
    PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS LIAVREHKAG 250
    EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR 300
    VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT 350
    SRVAMKYVD 359
    Length:359
    Mass (Da):39,153
    Last modified:June 7, 2005 - v1
    Checksum:iFDE9B438115342C2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381E → G in BAB71772. (PubMed:11676496)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB070927 Genomic DNA. Translation: BAB71772.1.
    AE005674 Genomic DNA. Translation: AAN45574.1.
    AE014073 Genomic DNA. Translation: AAP18624.1.
    RefSeqiNP_709867.1. NC_004337.2.
    NP_838813.1. NC_004741.1.

    Genome annotation databases

    EnsemblBacteriaiAAN45574; AAN45574; SF4152.
    AAP18624; AAP18624; S3578.
    GeneIDi1025471.
    1079800.
    KEGGisfl:SF4152.
    sfx:S3578.
    PATRICi18708936. VBIShiFle31049_3906.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB070927 Genomic DNA. Translation: BAB71772.1 .
    AE005674 Genomic DNA. Translation: AAN45574.1 .
    AE014073 Genomic DNA. Translation: AAP18624.1 .
    RefSeqi NP_709867.1. NC_004337.2.
    NP_838813.1. NC_004741.1.

    3D structure databases

    ProteinModelPortali P0A6B5.
    SMRi P0A6B5. Positions 1-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198214.SF4152.

    Chemistry

    BindingDBi P0A6B5.

    Proteomic databases

    PaxDbi P0A6B5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN45574 ; AAN45574 ; SF4152 .
    AAP18624 ; AAP18624 ; S3578 .
    GeneIDi 1025471.
    1079800.
    KEGGi sfl:SF4152.
    sfx:S3578.
    PATRICi 18708936. VBIShiFle31049_3906.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00042 ; UER00497 .
    UPA00219 .
    BRENDAi 5.1.1.1. 5712.

    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. "Gene cloning and characterization of alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei."
      Yokoigawa K., Hirasawa R., Ueno H., Okubo Y., Umesako S., Soda K.
      Biochem. Biophys. Res. Commun. 288:676-684(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    2. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
      Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
      , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
      Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 301 / Serotype 2a.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700930 / 2457T / Serotype 2a.

    Entry informationi

    Entry nameiALR1_SHIFL
    AccessioniPrimary (citable) accession number: P0A6B5
    Secondary accession number(s): P29743, P78136
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 73 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, Direct protein sequencing

    Documents

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

    External Data

    Dasty 3