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Entry version 121 (02 Jun 2021)
Sequence version 3 (08 May 2019)
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Protein

Broad specificity amino-acid racemase

Gene

bsrV

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Among these substrates, is the most efficient with lysine and arginine. Is also able to catalyze the racemization of several amino acids that are not typically incorporated into proteins such as ornithine and norleucine. Is not active on negatively charged (Glu and Asp) or aromatic (Tyr, Trp and Phe) amino acids and displays minimal activity towards beta-branched aliphatic (Ile, Val and Thr) substrates (PubMed:24419381).

Enables bacteria to produce and release extracellular non-canonical D-amino acids (NCDAAs) that regulate diverse cellular processes which may function as part of a cooperative strategy in vibrio communities to protect non-producing members from competing bacteria (PubMed:29446806, PubMed:29028003).

D-amino acid production by BsrV provides a cue for V.cholerae to decrease peptidoglycan synthesis and to alter its cell wall via incorporation of NCDAAs into the muropeptides, in adaption to stationary phase conditions (PubMed:19762646, PubMed:29028003).

1 Publication3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphateUniRule annotation1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 1.68 sec(-1) with L-alanine as substrate. kcat is 4.68 sec(-1) with L-serine as substrate. kcat is 2.94 sec(-1) with L-methionine as substrate. kcat is 2.30 sec(-1) with L-leucine as substrate. kcat is 2.59 sec(-1) with L-glutamine as substrate. kcat is 0.05 sec(-1) with L-asparagine as substrate. kcat is 4.76 sec(-1) with L-lysine as substrate. kcat is 5.09 sec(-1) with L-arginine as substrate.1 Publication
  1. KM=11 mM for L-alanine1 Publication
  2. KM=28 mM for L-serine1 Publication
  3. KM=11 mM for L-methionine1 Publication
  4. KM=30 mM for L-leucine1 Publication
  5. KM=22 mM for L-glutamine1 Publication
  6. KM=15 mM for L-asparagine1 Publication
  7. KM=9 mM for L-lysine1 Publication
  8. KM=18 mM for L-arginine1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei74Proton acceptorUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei173SubstrateUniRule annotation1
    Active sitei299Proton acceptorUniRule annotation1
    Binding sitei347Substrate; via amide nitrogenUniRule annotation1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei391Specificity determinant that enlarges the space within the active site of Bsr compared to Alr, allowing the accomodation of a wider range of substrates1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionIsomerase
    LigandPyridoxal phosphate

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Broad specificity amino-acid racemaseUniRule annotation1 Publication (EC:5.1.1.10UniRule annotation1 Publication)
    Alternative name(s):
    Broad spectrum racemase2 Publications
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:bsrV1 Publication
    Ordered Locus Names:VC_1312
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri243277 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Periplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    The substrate range of BsrV, which includes activity towards non-natural substrates (e.g. ornithine, norleucine, homoserine, N-acetyl lysine methyl ester, diaminobutyrate and aminobutyrate), is broader than any other known amino-acid racemase and suggests that it has great potential for biotechnological and industrial applications. Currently, production of DAA is an expensive process that is typically reliant upon inefficient chemical catalysts.1 Publication

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene have normal growth and morphology but produce minimal D-Met, D-Leu, D-Val, and D-Ile. They contain twice the amount of peptidoglycan (PG) of wild-type cells in stationary phase, whereas PG levels do not differ in exponential phase. Addition of physiological amounts of D-Met and D-Leu to cultures with a deletion in bsrV reduce the amount of PG to wild-type levels, which confirms that the absence of D-amino acids accounts for the increased PG in the bsrV mutant. Moreover, the structure of wild-type and bsrV mutant PG isolated from stationary phase cells differed significantly. The glycan chains in stationary phase PG from the bsrV mutant are about 80% the length of the wild type, pentapeptides are reduced by about 50%, and there is an increase in trimer muropeptides. Despite being less abundant, the PG in wild-type cells appears to be stronger than in bsrV mutant cells. Wild-type cells survive 20 times more than bsrV mutant cells when subjected to an osmotic challenge (PubMed:19762646). D-Arg is not detected in the supernatant of cells lacking this gene. Production of other D-amino acids (for example, D-Leu) is also impaired in the deletion mutant (PubMed:29028003).2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi25P → E: Completely abolishes the catalytic activity towards Ala and Met and dramatically impairs (70% reduction) activity towards Arg. 1 Publication1
    Mutagenesisi70C → A: Completely abolishes or hihgly reduces the catalytic activity towards Ala, Ser and large aliphatic side chains, while activity towards basic amino acids is preserved. 1 Publication1
    Mutagenesisi119R → A: Hihgly reduces the catalytic activity towards Ala and Ser and completely abolishes activity towards Met, Leu, Asn, Gln, Lys and Arg. 1 Publication1
    Mutagenesisi121R → A: Completely abolishes or hihgly reduces the catalytic activity towards all the amino acids. 1 Publication1
    Mutagenesisi165A → K: Completely abolishes or hihgly reduces the catalytic activity towards all the amino acids except Gln. 1 Publication1
    Mutagenesisi167N → A: Completely abolishes or hihgly reduces the catalytic activity towards all the amino acids. 1 Publication1
    Mutagenesisi169G → A: Completely abolishes or hihgly reduces the catalytic activity towards all the amino acids except Gln and Arg. 1 Publication1
    Mutagenesisi173 – 174RN → AA: Completely abolishes or hihgly reduces the catalytic activity towards all the amino acids. 1 Publication2
    Mutagenesisi391P → N: Completely abolishes the catalytic activity towards Ala, Ser and large aliphatic side chains, while activity towards basic amino acids is preserved. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23UniRule annotationAdd BLAST23
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000011459224 – 407Broad specificity amino-acid racemaseUniRule annotationAdd BLAST384

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi70 ↔ 96UniRule annotationBy similarity
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei74N6-(pyridoxal phosphate)lysineUniRule annotationCombined sources1 Publication1

    Keywords - PTMi

    Disulfide bond

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    243277.VC_1312

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1407
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9KSE5

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the alanine racemase family. Bsr subfamily.UniRule annotationCurated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0787, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_028393_2_2_6

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd06826, PLPDE_III_AR2, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.40.37.10, 1 hit
    3.20.20.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02212, Bsr_racemase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    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
    IPR043698, Racemase_Bsr/Lyr

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00842, Ala_racemase_C, 1 hit
    PF01168, Ala_racemase_N, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00992, ALARACEMASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01005, Ala_racemase_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50621, SSF50621, 1 hit
    SSF51419, SSF51419, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00492, alr, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00395, ALANINE_RACEMASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9KSE5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MHFKATLLSL SIAATLPSFS LSAAPLHIDT ALPDAAQIQQ SNSWLEISLG
    60 70 80 90 100
    QFQSNIEQFK SHMNANTKIC AIMKADAYGN GIRGLMPTII AQGIPCVGVA
    110 120 130 140 150
    SNAEARAVRE SGFKGELIRV RSASLSEMSS ALDLNIEELI GTHQQALDLA
    160 170 180 190 200
    ELAKQSGKTL KVHIALNDGG MGRNGIDMTT EAGKKEAVSI ATQPSLSVVG
    210 220 230 240 250
    IMTHFPNYNA DEVRAKLAQF KESSTWLMQQ ANLKREEITL HVANSYTALN
    260 270 280 290 300
    VPEAQLDMVR PGGVLFGDLP TNPEYPSIVS FKTRVSSLHH LPKDSTVGYD
    310 320 330 340 350
    STFTTSRDSV LANLPVGYSD GYPRKMGNKA EVLINGQRAK VVGVTSMNTT
    360 370 380 390 400
    VVDVTEIKGV LPGQEVVLFG QQQKQSIAVS EMENNAELIF PELYTLWGTS

    NPRFYVK
    Length:407
    Mass (Da):44,066
    Last modified:May 8, 2019 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i61B86E8502172FC1
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAF94470 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AE003852 Genomic DNA Translation: AAF94470.1 Different initiation.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A82215

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_230956.2, NC_002505.1
    WP_000545503.1, NZ_LT906614.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAF94470; AAF94470; VC_1312

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    57739977

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vch:VC1312

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE003852 Genomic DNA Translation: AAF94470.1 Different initiation.
    PIRiA82215
    RefSeqiNP_230956.2, NC_002505.1
    WP_000545503.1, NZ_LT906614.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4BEQX-ray1.50A24-407[»]
    4BEUX-ray1.15A24-407[»]
    SMRiQ9KSE5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi243277.VC_1312

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    2614766

    Genome annotation databases

    EnsemblBacteriaiAAF94470; AAF94470; VC_1312
    GeneIDi57739977
    KEGGivch:VC1312

    Phylogenomic databases

    eggNOGiCOG0787, Bacteria
    HOGENOMiCLU_028393_2_2_6

    Family and domain databases

    CDDicd06826, PLPDE_III_AR2, 1 hit
    Gene3Di2.40.37.10, 1 hit
    3.20.20.10, 1 hit
    HAMAPiMF_02212, Bsr_racemase, 1 hit
    InterProiView protein in InterPro
    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
    IPR043698, Racemase_Bsr/Lyr
    PfamiView protein in Pfam
    PF00842, Ala_racemase_C, 1 hit
    PF01168, Ala_racemase_N, 1 hit
    PRINTSiPR00992, ALARACEMASE
    SMARTiView protein in SMART
    SM01005, Ala_racemase_C, 1 hit
    SUPFAMiSSF50621, SSF50621, 1 hit
    SSF51419, SSF51419, 1 hit
    TIGRFAMsiTIGR00492, alr, 1 hit
    PROSITEiView protein in PROSITE
    PS00395, ALANINE_RACEMASE, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBSR_VIBCH
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9KSE5
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: May 8, 2019
    Last modified: June 2, 2021
    This is version 121 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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