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Q97LM4

- MALH_CLOAB

UniProt

Q97LM4 - MALH_CLOAB

Protein

Maltose-6'-phosphate glucosidase MalH

Gene

malH

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Oct 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of O-alpha-linked disaccharide 6-phosphates, including maltose-6'P and all five phosphorylated isomers of sucrose, but not sucrose-6P. Does not hydrolyze beta-linked disaccharide 6-phosphates such as cellobiose-6'P and gentiobiose-6'P. Is involved in the dissimilation of maltose and related O-alpha-linked glucosides produced via the phosphoenolpyruvate-dependent sugar phosphotransferase system (PEP-PTS).

    Catalytic activityi

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

    Cofactori

    Binds 1 NAD per subunit.
    Binds 1 manganese ion per subunit.

    Kineticsi

    1. KM=28.4 µM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate1 Publication
    2. KM=1.92 mM for trehalulose-6'P1 Publication
    3. KM=0.82 mM for turanose-6'P1 Publication
    4. KM=1.11 mM for maltulose-6'P1 Publication
    5. KM=1.87 mM for leucrose-6'P1 Publication
    6. KM=2.47 mM for palatinose-6'P1 Publication
    7. KM=1.95 mM for maltose-6'P1 Publication

    Vmax=5.2 µmol/min/mg enzyme with p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate as substrate1 Publication

    Vmax=0.43 µmol/min/mg enzyme with trehalulose-6'P as substrate1 Publication

    Vmax=0.82 µmol/min/mg enzyme with turanose-6'P as substrate1 Publication

    Vmax=0.65 µmol/min/mg enzyme with maltulose-6'P as substrate1 Publication

    Vmax=0.12 µmol/min/mg enzyme with leucrose-6'P as substrate1 Publication

    Vmax=0.60 µmol/min/mg enzyme with palatinose-6'P as substrate1 Publication

    Vmax=0.49 µmol/min/mg enzyme with maltose-6'P as substrate1 Publication

    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. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Manganese, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciCACE272562:GJIH-574-MONOMER.
    BRENDAi3.2.1.122. 1452.
    SABIO-RKQ97LM4.

    Protein family/group databases

    CAZyiGH4. Glycoside Hydrolase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maltose-6'-phosphate glucosidase MalH (EC:3.2.1.122)
    Alternative name(s):
    6-phospho-alpha-glucosidase
    6-phospho-glucosidase
    Maltose-6-phosphate hydrolase
    Gene namesi
    Name:malH
    Ordered Locus Names:CA_C0533
    OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
    Taxonomic identifieri272562 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000000814: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1691C → S: Loss of activity. 1 Publication
    Mutagenesisi170 – 1701D → N: Loss of activity. 1 Publication
    Mutagenesisi171 – 1711M → V: Highly reduced activity. 1 Publication
    Mutagenesisi172 – 1721P → A: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Maltose-6'-phosphate glucosidase MalHPRO_0000169863Add
    BLAST

    Expressioni

    Inductioni

    By maltose and other alpha-glucosides, except sucrose.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi272562.CA_C0533.

    Structurei

    3D structure databases

    ProteinModelPortaliQ97LM4.
    SMRiQ97LM4. Positions 2-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Phylogenomic databases

    eggNOGiCOG1486.
    HOGENOMiHOG000239810.
    KOiK01232.
    OMAiVLAHIRV.
    OrthoDBiEOG632D2X.

    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.

    Q97LM4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKFSVVIAG GGSTFTPGIV LMLLDNMDKF PIRKLKFYDN DKERQAIVAG    50
    ACEIILKEKA PEIEFLATTN PKEAFTDVDF VMAHIRVGKY AMRELDEKIP 100
    LKYGVVGQET CGPGGIAYGM RSIGGVIEIL DYMEKYSPNA WMLNYSNPAA 150
    IVAEATRKLR PNSKILNICD MPIGIETRMA EILGLESRKE MTVKYYGLNH 200
    FGWWSDIRDK DGNDLMPKLK EHVKKYGYVA ENGDTQHTDA SWNDTFAKAK 250
    DVYAVDPSTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC 300
    KKVIENQSTK GCKMEIDEHA SYIVDLARAI SYNTHERMLL IVPNNGSIEN 350
    FDSTGMVEIP CIVGSNGPEP LTMGKIPQFQ KGLMEQQVSV EKLVVEAWKE 400
    KSYQKLWQAI TLSRTVPSAK VAKQILDELI EVNKDYWPEL N 441
    Length:441
    Mass (Da):49,972
    Last modified:October 1, 2001 - v1
    Checksum:iB525EE15EC0CD69E
    GO

    Mass spectrometryi

    Molecular mass is 49973 Da from positions 1 - 441. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF290982 Genomic DNA. Translation: AAK69556.1.
    AE001437 Genomic DNA. Translation: AAK78512.1.
    PIRiE96965.
    RefSeqiNP_347172.1. NC_003030.1.
    WP_010963854.1. NC_003030.1.

    Genome annotation databases

    EnsemblBacteriaiAAK78512; AAK78512; CA_C0533.
    GeneIDi1116716.
    KEGGicac:CA_C0533.
    PATRICi32035429. VBICloAce74127_0736.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF290982 Genomic DNA. Translation: AAK69556.1 .
    AE001437 Genomic DNA. Translation: AAK78512.1 .
    PIRi E96965.
    RefSeqi NP_347172.1. NC_003030.1.
    WP_010963854.1. NC_003030.1.

    3D structure databases

    ProteinModelPortali Q97LM4.
    SMRi Q97LM4. Positions 2-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272562.CA_C0533.

    Protein family/group databases

    CAZyi GH4. Glycoside Hydrolase Family 4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK78512 ; AAK78512 ; CA_C0533 .
    GeneIDi 1116716.
    KEGGi cac:CA_C0533.
    PATRICi 32035429. VBICloAce74127_0736.

    Phylogenomic databases

    eggNOGi COG1486.
    HOGENOMi HOG000239810.
    KOi K01232.
    OMAi VLAHIRV.
    OrthoDBi EOG632D2X.

    Enzyme and pathway databases

    BioCyci CACE272562:GJIH-574-MONOMER.
    BRENDAi 3.2.1.122. 1452.
    SABIO-RK Q97LM4.

    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. "Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824."
      Tangney M., Winters G.T., Mitchell W.J.
      J. Ind. Microbiol. Biotechnol. 27:298-306(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
    3. "Genes malh and pagl of Clostridium acetobutylicum ATCC 824 encode NAD+- and Mn2+-dependent phospho-alpha-glucosidase(s)."
      Thompson J., Hess S., Pikis A.
      J. Biol. Chem. 279:1553-1561(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-29, CHARACTERIZATION, KINETIC PARAMETERS, MUTAGENESIS OF CYS-169; ASP-170; MET-171 AND PRO-172, MASS SPECTROMETRY.
      Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

    Entry informationi

    Entry nameiMALH_CLOAB
    AccessioniPrimary (citable) accession number: Q97LM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 79 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3