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Entry version 103 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Bcs1

Gene

bcs1

Organism
Haemophilus influenzae
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

Catalyzes the NADPH-dependent reduction of D-ribulose 5-phosphate to D-ribitol 5-phosphate and the further reaction of D-ribitol 5-phosphate with CTP to form CDP-ribitol.2 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 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 22 sec(-1) for the reductase reaction. kcat is 13 sec(-1) for the cytidyltransferase reaction.1 Publication
  1. KM=42 µM for D-ribulose 5-phosphate1 Publication
  2. KM=106 µM for D-ribulose 5-phosphate1 Publication
  3. KM=25 µM for NADPH1 Publication
  4. KM=7.06 µM for NADPH1 Publication
  5. KM=75 µM for D-ribitol 5-phosphate (for the cytidylyltransferase reaction)1 Publication
  6. KM=14.7 µM for D-ribitol 5-phosphate (for the cytidylyltransferase reaction)1 Publication
  7. KM=74 µM for CTP1 Publication
  8. KM=8.51 µM for CTP1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: capsule polysaccharide biosynthesis

    This protein is involved in the pathway capsule polysaccharide biosynthesis, which is part of Capsule biogenesis.Curated
    View all proteins of this organism that are known to be involved in the pathway capsule polysaccharide biosynthesis and in Capsule biogenesis.

    <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 functionNucleotidyltransferase, Oxidoreductase, Transferase
    Biological processCapsule biogenesis/degradation
    LigandNADP

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q48230

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00934

    <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:
    Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Bcs1Curated
    Alternative name(s):
    CDP-ribitol synthase1 Publication
    Including the following 2 domains:
    Ribitol-5-phosphate cytidylyltransferase1 Publication (EC:2.7.7.402 Publications)
    Ribulose-5-phosphate reductase1 Publication (EC:1.1.1.4052 Publications)
    Short name:
    Ribulose-5-P reductaseCurated
    Alternative name(s):
    Ribitol-5-phosphate dehydrogenaseCurated
    <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:bcs1Imported
    <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>OrganismiHaemophilus influenzaeImported
    <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 identifieri727 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

    <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

    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>Mutagenesisi18R → A: Has 100-fold reduction of catalytic efficiency for the cytidylyltransferase activity. 1 Publication1
    Mutagenesisi386K → A: Has 70-fold reduction of catalytic efficiency for the reductase activity. 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 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_00004375061 – 474Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Bcs1Add BLAST474

    <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

    Monomer.

    2 Publications

    <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

    3D structure databases

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

    More...
    SMRi
    Q48230

    Database of comparative protein structure models

    More...
    ModBasei
    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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 238Ribitol-5-phosphate cytidylyltransferaseAdd BLAST238
    Regioni250 – 474Ribulose-5-phosphate reductaseAdd BLAST225

    <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

    In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family.Curated
    In the C-terminal section; belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02516, CDP-ME_synthetase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.90.550.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00108, IspD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR012115, CDP-ribitol_syn
    IPR001228, IspD
    IPR034683, IspD/TarI
    IPR036291, NAD(P)-bd_dom_sf
    IPR029044, Nucleotide-diphossugar_trans
    IPR020904, Sc_DH/Rdtase_CS
    IPR002347, SDR_fam

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01128, IspD, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF036586, CDP-ribitol_syn, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00081, GDHRDH

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735, SSF51735, 1 hit
    SSF53448, SSF53448, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00061, ADH_SHORT, 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.

    Q48230-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNKNKNIGII LAGGVGSRMG LGYPKQFSKI AGKTALEHTL AIFQEHKEID
    60 70 80 90 100
    EIIIVSERTS YRRIEDIVSK LDFSKVNRII FGGKERSDST LSAITALQDE
    110 120 130 140 150
    PENTKLIIHD AVRPLLATEI ISECIAKLDK YNAVDVAIPA VDTIVHVNND
    160 170 180 190 200
    TQEIIKIPKR AEYYQGQTPQ AFKLGTLKKA YDIYTQGGIE GTCDCSIVLK
    210 220 230 240 250
    TLPEERVGIV SGSETNIKLT RPVDLFIADK LFQSRSHFSL RNITSIDRLY
    260 270 280 290 300
    DMKDQVLVVI GGSYGIGAHI IDIAKKFGIK TYSLSRSNGV DVGDVKSIEK
    310 320 330 340 350
    AFAEIYAKEH KIDHIVNTAA VLNHKTLVSM SYEEILTSIN VNYTGMINAV
    360 370 380 390 400
    ITAYPYLKQT HGSFLGFTSS SYTRGRPFYA IYSSAKAAVV NLTQAISEEW
    410 420 430 440 450
    LPDNIKINCV NPERTKTPMR TKAFGIEPEG TLLDAKTVAF ASLVVLASRE
    460 470
    TGNIIDVVLK DEEYITNILA DLYK
    Length:474
    Mass (Da):52,467
    Last modified:November 1, 1996 - v1
    <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:iDC42A2B245318A95
    GO

    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
    AF549210 Genomic DNA Translation: AAP42161.1
    AF549212 Genomic DNA Translation: AAP42171.1
    X78559 Genomic DNA Translation: CAA55303.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S60902

    <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
    AF549210 Genomic DNA Translation: AAP42161.1
    AF549212 Genomic DNA Translation: AAP42171.1
    X78559 Genomic DNA Translation: CAA55303.1
    PIRiS60902

    3D structure databases

    SMRiQ48230
    ModBaseiSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00934
    SABIO-RKiQ48230

    Family and domain databases

    CDDicd02516, CDP-ME_synthetase, 1 hit
    Gene3Di3.90.550.10, 1 hit
    HAMAPiMF_00108, IspD, 1 hit
    InterProiView protein in InterPro
    IPR012115, CDP-ribitol_syn
    IPR001228, IspD
    IPR034683, IspD/TarI
    IPR036291, NAD(P)-bd_dom_sf
    IPR029044, Nucleotide-diphossugar_trans
    IPR020904, Sc_DH/Rdtase_CS
    IPR002347, SDR_fam
    PfamiView protein in Pfam
    PF01128, IspD, 1 hit
    PIRSFiPIRSF036586, CDP-ribitol_syn, 1 hit
    PRINTSiPR00081, GDHRDH
    SUPFAMiSSF51735, SSF51735, 1 hit
    SSF53448, SSF53448, 1 hit
    PROSITEiView protein in PROSITE
    PS00061, ADH_SHORT, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiBCS1_HAEIF
    <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: Q48230
    <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: October 5, 2016
    Last sequence update: November 1, 1996
    Last modified: December 11, 2019
    This is version 103 of the entry and version 1 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

    Documents

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