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Q46769

- RMLD_ECOLX

UniProt

Q46769 - RMLD_ECOLX

Protein

dTDP-4-dehydrorhamnose reductase

Gene

rfbD

Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well.1 Publication

    Catalytic activityi

    dTDP-beta-L-rhamnose + NADP+ = dTDP-4-dehydro-beta-L-rhamnose + NADPH.

    Cofactori

    Binds 1 magnesium ion per monomer.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121NAD; via amide nitrogenBy similarity
    Binding sitei102 – 1021NADP; via carbonyl oxygenBy similarity
    Binding sitei155 – 1551Substrate; via amide nitrogenBy similarity
    Binding sitei156 – 1561NAD; via amide nitrogenBy similarity
    Binding sitei225 – 2251SubstrateBy similarity
    Binding sitei262 – 2621SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 115NADBy similarity
    Nucleotide bindingi11 – 122NADPBy similarity
    Nucleotide bindingi30 – 312NADBy similarity
    Nucleotide bindingi39 – 402NAD/NADPBy similarity
    Nucleotide bindingi62 – 654NADBy similarity
    Nucleotide bindingi63 – 653NADPBy similarity
    Nucleotide bindingi129 – 1335NAD/NADPBy similarity

    GO - Molecular functioni

    1. dTDP-4-dehydrorhamnose reductase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
    2. extracellular polysaccharide biosynthetic process Source: UniProtKB
    3. lipopolysaccharide biosynthetic process Source: UniProtKB
    4. O antigen biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipopolysaccharide biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding, NADP

    Enzyme and pathway databases

    UniPathwayiUPA00124.
    UPA00281.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    dTDP-4-dehydrorhamnose reductase (EC:1.1.1.133)
    Alternative name(s):
    dTDP-4-keto-L-rhamnose reductase
    dTDP-6-deoxy-L-lyxo-4-hexulose reductase
    dTDP-6-deoxy-L-mannose dehydrogenase
    dTDP-L-rhamnose synthase
    Gene namesi
    Name:rfbD
    Synonyms:rmlD
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 301301dTDP-4-dehydrorhamnose reductasePRO_0000207985Add
    BLAST

    Proteomic databases

    PaxDbiQ46769.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ46769.
    SMRiQ46769. Positions 1-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni104 – 1052Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1091.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005913. dTDP_dehydrorham_reduct.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF04321. RmlD_sub_bind. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01214. rmlD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q46769-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNILLFGKTG QVGWELQRAL APLGNLIALD VHSTDYCGDF SNPEGVAETV    50
    KKIRPDVIVN AAAHTDVDKA ESEPEFAQLL NATSVEAIAK AANEVGAWVI 100
    HYSTDYVFPG TGEIPWQGGT DATAPLNVYG ETKLSSEKKA LQKHCGKHII 150
    FRTSWVYAGK GNNFAKTMLR LAKEREELAV INDQFGRPTG AELLADCTAH 200
    AIRVAVDKPE VAGLYHLVAG GTTTWHDYAA LVFEEARKAG INLALNKLNA 250
    VPTTAYPTPA RRPHNSRLNT EKFQQNFALV LPDWQVGVKR MLNELFTTTA 300
    I 301
    Length:301
    Mass (Da):32,866
    Last modified:November 1, 1996 - v1
    Checksum:iA1C4271C20AB4A13
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF125322 Genomic DNA. Translation: AAC63613.1.
    PIRiS78543.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF125322 Genomic DNA. Translation: AAC63613.1 .
    PIRi S78543.

    3D structure databases

    ProteinModelPortali Q46769.
    SMRi Q46769. Positions 1-299.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q46769.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1091.

    Enzyme and pathway databases

    UniPathwayi UPA00124 .
    UPA00281 .

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR005913. dTDP_dehydrorham_reduct.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF04321. RmlD_sub_bind. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01214. rmlD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene."
      Marolda C.L., Valvano M.A.
      J. Bacteriol. 177:5539-5546(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS.
      Strain: O7:K1 / VW187.

    Entry informationi

    Entry nameiRMLD_ECOLX
    AccessioniPrimary (citable) accession number: Q46769
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3