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Q9AI65

- PALH_ERWRD

UniProt

Q9AI65 - PALH_ERWRD

Protein

Alpha-glucosidase

Gene

palH

Organism
Erwinia rhapontici (Pectobacterium rhapontici)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    Alpha-glucosidase with broad specificity. Hydrolyzes maltose, palatinose, maltulose, trehalose, trehalulose, turanose, leucrose, sucrose and maltitol. Is not active against alpha-galactosides, e.g. melibiose, and alpha-mannosides. Shows an obligate requirement for an O-alpha-glycosidic linkage, since it is not able to cleave beta-glycosidic bonds (cellobiose, gentiobiose, lactose, sophorose or laminaribiose). Can not hydrolyze phosphorylated alpha-glucosides derivatives. Seems to be involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.1 Publication

    Catalytic activityi

    Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.1 Publication

    Cofactori

    Binds 1 divalent metal ion per subunit. Mn2+ is the most efficient metal, but to a lesser extent, can also use Co2+, Ca2+, Fe2+, Mg2+, Sr2+, and Ni2+. Can not use Zn2+, Cu2+ or Cr2+.1 Publication
    Binds 1 NAD+ per subunit.1 Publication

    Enzyme regulationi

    Is inhibited by EDTA in vitro.1 Publication

    Kineticsi

    1. KM=8.58 mM for maltose1 Publication
    2. KM=7.31 mM for maltitol1 Publication
    3. KM=6.59 mM for trehalose1 Publication
    4. KM=3.63 mM for trehalulose1 Publication
    5. KM=22.11 mM for sucrose1 Publication
    6. KM=10.04 mM for turanose1 Publication
    7. KM=1.75 mM for maltulose1 Publication
    8. KM=5.31 mM for leucrose1 Publication
    9. KM=2.52 mM for palatinose1 Publication
    10. KM=180 µM for 4-nitrophenyl-alpha-D-glucopyranoside1 Publication
    11. KM=104 µM for NAD+1 Publication
    12. KM=47.2 µM for Mn2+1 Publication

    Vmax=1.01 µmol/min/mg enzyme with maltose as substrate1 Publication

    Vmax=0.24 µmol/min/mg enzyme with maltitol as substrate1 Publication

    Vmax=0.51 µmol/min/mg enzyme with trehalose as substrate1 Publication

    Vmax=0.47 µmol/min/mg enzyme with trehalulose as substrate1 Publication

    Vmax=0.31 µmol/min/mg enzyme with sucrose as substrate1 Publication

    Vmax=0.46 µmol/min/mg enzyme with turanose as substrate1 Publication

    Vmax=0.53 µmol/min/mg enzyme with maltulose as substrate1 Publication

    Vmax=0.44 µmol/min/mg enzyme with leucrose as substrate1 Publication

    Vmax=0.70 µmol/min/mg enzyme with palatinose as substrate1 Publication

    Vmax=6.01 µmol/min/mg enzyme with 4-nitrophenyl-alpha-D-glucopyranoside as substrate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei149 – 1491SubstrateBy similarity
    Metal bindingi171 – 1711ManganeseBy similarity
    Active sitei172 – 1721Proton donorBy similarity
    Metal bindingi201 – 2011ManganeseBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi3 – 6967NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. maltose alpha-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

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

    Enzyme and pathway databases

    UniPathwayiUPA01004.

    Protein family/group databases

    CAZyiGH4. Glycoside Hydrolase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucosidase (EC:3.2.1.20)
    Gene namesi
    Name:palH
    OrganismiErwinia rhapontici (Pectobacterium rhapontici)
    Taxonomic identifieri55212 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi173 – 1731E → S: Loss of catalytic activity. 1 Publication
    Mutagenesisi174 – 1741I → V: No effect on catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 453452Alpha-glucosidasePRO_0000389548Add
    BLAST

    Expressioni

    Inductioni

    Down-regulated by sucrose and up-regulated by palatinose.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9AI65.
    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.
    InterProiIPR001088. 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.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9AI65-1 [UniParc]FASTAAdd to Basket

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    MATKIVLVGA GSAQFGYGTL GDIFQSRALY GSEIILHDIN PVALAVTEKT    50
    AKDFLAKEDL PFIVSATTDR RTALRGAEFV IISIEVGDRF ALWDLDWQIP 100
    QQYGIQQVYG ENGGPGGLFH SLRIIPPILD ICADVADICP DAWIFNYSNP 150
    MSRICTTVHR RFPELNFVGM CHEIASLERY LPEMLNTSFD NLSLRAGGLN 200
    HFSVLLDARY KDSGKDAYAD VRAKAPDYFA SLPGYSDILA YTRQHGKLVD 250
    TEGSTERHAL GGKDSSYPWA DRTLFKEILE KFHCMPITVD SHFGEYISWA 300
    GEVSDHRGIL DFYTFYRNYL GGVQPKIELK LKERVVSIME GILTDSGYEE 350
    AAVNIPNRGF IKQLPEFIAV EVPAIIDRKG VHGIQVDIPP GIGGLLSNQI 400
    AIHDLTAEAI IAGSRDLVIQ ALLVDSVNNQ CRAIPELVDV MISRQQPWLN 450
    YLK 453
    Length:453
    Mass (Da):50,341
    Last modified:November 24, 2009 - v2
    Checksum:i64B178085AE436AC
    GO

    Sequence cautioni

    The sequence AAK28734.1 differs from that shown. Reason: Erroneous initiation.

    Mass spectrometryi

    Molecular mass is 50216 Da from positions 2 - 453. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF279280 Genomic DNA. Translation: AAK28734.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF279280 Genomic DNA. Translation: AAK28734.1 . Different initiation.

    3D structure databases

    ProteinModelPortali Q9AI65.
    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 UPA01004 .

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProi 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.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the gene cluster for palatinose metabolism from the phytopathogenic bacterium Erwinia rhapontici."
      Boernke F., Hajirezaei M., Sonnewald U.
      J. Bacteriol. 183:2425-2430(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PALATINOSE METABOLISM, PATHWAY, INDUCTION.
      Strain: ATCC 29283 / DSM 4484 / NCPPB 1578 / ICPB ER 102.
    2. "Evolution and biochemistry of family 4 glycosidases: implications for assigning enzyme function in sequence annotations."
      Hall B.G., Pikis A., Thompson J.
      Mol. Biol. Evol. 26:2487-2497(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ENZYME REGULATION, KINETIC PARAMETERS, MASS SPECTROMETRY, SUBUNIT, MUTAGENESIS OF GLU-173 AND ILE-174.
      Strain: ATCC 29283 / DSM 4484 / NCPPB 1578 / ICPB ER 102.

    Entry informationi

    Entry nameiPALH_ERWRD
    AccessioniPrimary (citable) accession number: Q9AI65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 47 of the entry and version 2 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