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Protein

Beta-1,4-mannooligosaccharide phosphorylase

Gene

Rumal_0099

Organism
Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorolysis of beta-1,4-mannooligosaccharides to mannose 1-phosphate (Man1P) and shorter mannooligosaccharides. Can also catalyze the phosphorolysis of 4-O-beta-D-mannopyranosyl-D-glucopyranose (Man-Glc), but shows higher activity toward longer mannooligosaccharides. Involved in a mannan catabolic pathway which feeds into glycolysis.1 Publication

Miscellaneous

Both RaMP1 (Rumal_0852) and RaMP2 catalyze the phosphorolysis of a beta-1,4-mannosidic linkage at the non-reducing end of a substrate, but acceptor specificities are clearly different.1 Publication

Catalytic activityi

((1->4)-beta-D-mannosyl)(n) + phosphate = ((1->4)-beta-D-mannosyl)(n-1) + alpha-D-mannose 1-phosphate.1 Publication

Kineticsi

kcat is 20.7 sec(-1) for Man-Glc. kcat is 7.06 sec(-1) for beta-1,4-mannobiose. kcat is 27.5 sec(-1) for beta-1,4-mannotriose. kcat is 33.1 sec(-1) for beta-1,4-mannotetraose. kcat is 31.9 sec(-1) for beta-1,4-mannopentaose.
  1. KM=28.4 mM for Man-Glc1 Publication
  2. KM=44.5 mM for beta-1,4-mannobiose1 Publication
  3. KM=7.94 mM for beta-1,4-mannotriose1 Publication
  4. KM=3.21 mM for beta-1,4-mannotetraose1 Publication
  5. KM=4.55 mM for beta-1,4-mannopentaose1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase
    Biological processCarbohydrate metabolism, Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18534
    BRENDAi2.4.1.281 5477
    2.4.1.319 5477

    Protein family/group databases

    CAZyiGH130 Glycoside Hydrolase Family 130

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-1,4-mannooligosaccharide phosphorylase (EC:2.4.1.319)
    Alternative name(s):
    RaMP2
    Gene namesi
    Ordered Locus Names:Rumal_0099
    OrganismiRuminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7)
    Taxonomic identifieri697329 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminococcus
    Proteomesi
    • UP000006919 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004213651 – 335Beta-1,4-mannooligosaccharide phosphorylaseAdd BLAST335

    Interactioni

    Subunit structurei

    Homohexamer in solution.1 Publication

    Protein-protein interaction databases

    MINTiE6UBR9
    STRINGi697329.Rumal_0099

    Structurei

    Secondary structure

    1335
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 7Combined sources3
    Beta strandi25 – 29Combined sources5
    Beta strandi44 – 57Combined sources14
    Beta strandi60 – 70Combined sources11
    Beta strandi75 – 87Combined sources13
    Beta strandi98 – 101Combined sources4
    Helixi102 – 104Combined sources3
    Turni105 – 108Combined sources4
    Beta strandi113 – 121Combined sources9
    Beta strandi124 – 152Combined sources29
    Beta strandi159 – 166Combined sources8
    Beta strandi174 – 181Combined sources8
    Beta strandi184 – 186Combined sources3
    Beta strandi192 – 210Combined sources19
    Helixi215 – 217Combined sources3
    Beta strandi218 – 223Combined sources6
    Beta strandi228 – 230Combined sources3
    Beta strandi233 – 244Combined sources12
    Beta strandi247 – 257Combined sources11
    Beta strandi259 – 261Combined sources3
    Beta strandi264 – 271Combined sources8
    Helixi279 – 282Combined sources4
    Beta strandi283 – 298Combined sources16
    Turni299 – 301Combined sources3
    Beta strandi303 – 310Combined sources8
    Turni311 – 313Combined sources3
    Beta strandi314 – 321Combined sources8
    Helixi322 – 331Combined sources10

    3D structure databases

    SMRiE6UBR9
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 130 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CKB Bacteria
    COG2152 LUCA
    HOGENOMiHOG000268565
    KOiK18785
    OMAiEKFYQIE
    OrthoDBiPOG091H0J20

    Family and domain databases

    Gene3Di2.115.10.20, 1 hit
    InterProiView protein in InterPro
    IPR023296 Glyco_hydro_beta-prop_sf
    IPR007184 Mannoside_phosphorylase
    PANTHERiPTHR34106 PTHR34106, 1 hit
    PfamiView protein in Pfam
    PF04041 Glyco_hydro_130, 1 hit
    PIRSFiPIRSF016202 PH1107, 1 hit
    SUPFAMiSSF75005 SSF75005, 1 hit

    Sequencei

    Sequence statusi: Complete.

    E6UBR9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTQIINGVS LPNIPWQDKP ADCKDVIWRY DANPIIPRDQ LPTSNSIFNS
    60 70 80 90 100
    AVVPYESEKG KFAGVFRVDD KCRNMELHAG FSKDGIHWDI NPDRIVFEQA
    110 120 130 140 150
    EKSTEEVNQW GYGYDPRVCF IEDRFWVTWC NAYGWKPTIG VAYTFDFKTF
    160 170 180 190 200
    YQCENAFLPF NRNGVLFPRK INGKYVMFSR PSDSGHTPFG DMFISQSPDM
    210 220 230 240 250
    KYWGEHRHVM GPLRAWESKK IGAGPIPIET SEGWLCFYHG VLESCNGFVY
    260 270 280 290 300
    SFSACILDKD EPWKVKYRCA EYLLSPQKIY ECVGDVQNVT FPCATLVDAD
    310 320 330
    TGRIAIYYGC ADTCVSMAFT TVDDVVDYVK SHSSV
    Length:335
    Mass (Da):38,311
    Last modified:March 8, 2011 - v1
    Checksum:i0F6B3CF6A67DEC8B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP002403 Genomic DNA Translation: ADU20661.1
    RefSeqiWP_013496855.1, NZ_JHYT01000018.1

    Genome annotation databases

    EnsemblBacteriaiADU20661; ADU20661; Rumal_0099
    KEGGiral:Rumal_0099

    Similar proteinsi

    Entry informationi

    Entry nameiMOSP_RUMA7
    AccessioniPrimary (citable) accession number: E6UBR9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2013
    Last sequence update: March 8, 2011
    Last modified: July 18, 2018
    This is version 38 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

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