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Q9AI65

- PALH_ERWRD

UniProt

Q9AI65 - PALH_ERWRD

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Protein

Alpha-glucosidase

Gene
palH
Organism
Erwinia rhapontici (Pectobacterium rhapontici)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 maltitol
  3. KM=6.59 mM for trehalose
  4. KM=3.63 mM for trehalulose
  5. KM=22.11 mM for sucrose
  6. KM=10.04 mM for turanose
  7. KM=1.75 mM for maltulose
  8. KM=5.31 mM for leucrose
  9. KM=2.52 mM for palatinose
  10. KM=180 µM for 4-nitrophenyl-alpha-D-glucopyranoside
  11. KM=104 µM for NAD+
  12. KM=47.2 µM for Mn2+

Vmax=1.01 µmol/min/mg enzyme with maltose as substrate

Vmax=0.24 µmol/min/mg enzyme with maltitol as substrate

Vmax=0.51 µmol/min/mg enzyme with trehalose as substrate

Vmax=0.47 µmol/min/mg enzyme with trehalulose as substrate

Vmax=0.31 µmol/min/mg enzyme with sucrose as substrate

Vmax=0.46 µmol/min/mg enzyme with turanose as substrate

Vmax=0.53 µmol/min/mg enzyme with maltulose as substrate

Vmax=0.44 µmol/min/mg enzyme with leucrose as substrate

Vmax=0.70 µmol/min/mg enzyme with palatinose as substrate

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei149 – 1491Substrate By similarity
Metal bindingi171 – 1711Manganese By similarity
Active sitei172 – 1721Proton donor By similarity
Metal bindingi201 – 2011Manganese By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi3 – 6967NAD By 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
Complete GO annotation...

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.2 Publications

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9AI65.

Family & Domainsi

Sequence similaritiesi

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: February 19, 2014
This is version 46 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

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