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O06901

- MALH_FUSMR

UniProt

O06901 - MALH_FUSMR

Protein

Maltose-6'-phosphate glucosidase

Gene

malH

Organism
Fusobacterium mortiferum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides including maltose-6'P, trehalose-6P and the 6'-phosphorylated derivatives of the five linkage-isomeric alpha-D-glucosyl-D-fructoses: trehalulose-6'P, turanose-6'P, maltulose-6'P, leucrose-6'P, and palatinose-6'P. However, sucrose-6P is not a substrate for MalH, and this enzyme also fails to hydrolyze beta-O-linked phosphorylated disaccharides such as cellobiose-6'P and gentobiose-6'P.

    Catalytic activityi

    Alpha-maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate.

    Cofactori

    NAD.
    Divalent metal ion. Manganese, iron, cobalt and nickel ions enhance activity whereas magnesium, zinc, calcium and strontium do not.

    pH dependencei

    Optimum pH is 7.0-7.5.

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei93 – 931SubstrateBy similarity
    Sitei109 – 1091Increases basicity of active site TyrBy similarity
    Binding sitei147 – 1471SubstrateBy similarity
    Metal bindingi169 – 1691ManganeseBy similarity
    Active sitei170 – 1701Proton donorBy similarity
    Metal bindingi200 – 2001ManganeseBy similarity
    Active sitei264 – 2641Proton acceptorBy similarity
    Binding sitei284 – 2841SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 7067NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. maltose-6'-phosphate glucosidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

    GO - Biological processi

    1. maltose catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Cobalt, Iron, Manganese, Metal-binding, NAD, Nickel

    Enzyme and pathway databases

    BRENDAi3.2.1.122. 2369.
    SABIO-RKO06901.
    UniPathwayiUPA00150.

    Protein family/group databases

    CAZyiGH4. Glycoside Hydrolase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maltose-6'-phosphate glucosidase (EC:3.2.1.122)
    Alternative name(s):
    6-phospho-alpha-D-glucosidase
    Gene namesi
    Name:malH
    OrganismiFusobacterium mortiferum
    Taxonomic identifieri850 [NCBI]
    Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Maltose-6'-phosphate glucosidasePRO_0000169864Add
    BLAST

    Expressioni

    Inductioni

    By the five sucrose isomers and other alpha-glucosides (but not by sucrose or glucose).

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO06901.
    SMRiO06901. Positions 2-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProiIPR019802. GlycHydrolase_4_CS.
    IPR001088. Glyco_hydro_4.
    IPR022616. Glyco_hydro_4_C.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view]
    PRINTSiPR00732. GLHYDRLASE4.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O06901-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKQFSILIAG GGSTFTPGII LMLLDNLDKF PIRQIKMFDN DAERQAKIGE    50
    ACAILLKEKA PQIKFSYSTN PEEAFTDIDF VMAHIRVGKY PMRELDEKIP 100
    LRHGVVGQET CGPGGIAYGM RSIGGVIGLI DYMEKYSPNA WMLNYSNPAA 150
    IVAEATRRLR PNSKVLNICD MPIGIEVRMA EILGLESRKD MDIMYYGLNH 200
    FGWWKSVRDK QGNDLMPKLR EHVSQYGYVV PKGDNQHTEA SWNDTFAKAK 250
    DVLALDPTTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC 300
    EKVVKNQSSE GCALHIDEHA SYIVDLARAI AFNTKEKMLL IVENNGAIVN 350
    FDSTAMVEIP CIVGSNGPEP LVVGRIPQFQ KGMMEQQVTV EKLTVEAWIE 400
    GSYQKLWQAI TMSKTVPSAK VAKDILDDLI EANKEYWPVL K 441
    Length:441
    Mass (Da):49,712
    Last modified:July 1, 1997 - v1
    Checksum:iEE9D85B35FA8AF46
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81185 Genomic DNA. Translation: AAB63015.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81185 Genomic DNA. Translation: AAB63015.1 .

    3D structure databases

    ProteinModelPortali O06901.
    SMRi O06901. Positions 2-440.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH4. Glycoside Hydrolase Family 4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00150 .
    BRENDAi 3.2.1.122. 2369.
    SABIO-RK O06901.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProi IPR019802. GlycHydrolase_4_CS.
    IPR001088. Glyco_hydro_4.
    IPR022616. Glyco_hydro_4_C.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view ]
    PRINTSi PR00732. GLHYDRLASE4.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    PROSITEi PS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "6-phospho-alpha-D-glucosidase from Fusobacterium mortiferum: cloning, expression, and assignment to family 4 of the glycosylhydrolases."
      Bouma C.L., Reizer J., Reizer A., Robrish S.A., Thompson J.
      J. Bacteriol. 179:4129-4137(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 25557 / CCUG 14475.
    2. "Purification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-alpha-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyzes maltose 6-phosphate and related phospho-alpha-D-glucosides."
      Thompson J., Gentry-Weeks C.R., Nguyen N.Y., Folk J.E., Robrish S.A.
      J. Bacteriol. 177:2505-2512(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-32, CHARACTERIZATION.
      Strain: ATCC 25557 / CCUG 14475.
    3. "Metabolism of sucrose and its five isomers by Fusobacterium mortiferum."
      Pikis A., Immel S., Robrish S.A., Thompson J.
      Microbiology 148:843-852(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
      Strain: ATCC 25557 / CCUG 14475.

    Entry informationi

    Entry nameiMALH_FUSMR
    AccessioniPrimary (citable) accession number: O06901
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 77 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

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3