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Protein

Alpha-glucosidase

Gene

palH

Organism
Erwinia rhapontici (Pectobacterium rhapontici)
Status
Reviewed-Annotation score: 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). Cannot 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

Protein has several cofactor binding sites:
  • Mn2+1 Publication, Co2+1 Publication, Ca2+1 Publication, Fe2+1 Publication, Mg2+1 Publication, Sr2+1 Publication, Ni2+1 PublicationNote: 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+. Cannot use Zn2+, Cu2+ or Cr2+.1 Publication
  • NAD+1 PublicationNote: 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
  1. Vmax=1.01 µmol/min/mg enzyme with maltose as substrate1 Publication
  2. Vmax=0.24 µmol/min/mg enzyme with maltitol as substrate1 Publication
  3. Vmax=0.51 µmol/min/mg enzyme with trehalose as substrate1 Publication
  4. Vmax=0.47 µmol/min/mg enzyme with trehalulose as substrate1 Publication
  5. Vmax=0.31 µmol/min/mg enzyme with sucrose as substrate1 Publication
  6. Vmax=0.46 µmol/min/mg enzyme with turanose as substrate1 Publication
  7. Vmax=0.53 µmol/min/mg enzyme with maltulose as substrate1 Publication
  8. Vmax=0.44 µmol/min/mg enzyme with leucrose as substrate1 Publication
  9. Vmax=0.70 µmol/min/mg enzyme with palatinose as substrate1 Publication
  10. Vmax=6.01 µmol/min/mg enzyme with 4-nitrophenyl-alpha-D-glucopyranoside as substrate1 Publication

Pathwayi: palatinose degradation

This protein is involved in the pathway palatinose degradation, which is part of Glycan degradation.1 Publication
View all proteins of this organism that are known to be involved in the pathway palatinose degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei149SubstrateBy similarity1
Metal bindingi171ManganeseBy similarity1
Active sitei172Proton donorBy similarity1
Metal bindingi201ManganeseBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi3 – 69NADBy similarityAdd BLAST67

GO - Molecular functioni

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

BRENDAi3.2.1.20. 2149.
3.2.1.86. 2149.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeErwinia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi173E → S: Loss of catalytic activity. 1 Publication1
Mutagenesisi174I → V: No effect on catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003895482 – 453Alpha-glucosidaseAdd BLAST452

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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. 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

« Hide

        10         20         30         40         50
MATKIVLVGA GSAQFGYGTL GDIFQSRALY GSEIILHDIN PVALAVTEKT
60 70 80 90 100
AKDFLAKEDL PFIVSATTDR RTALRGAEFV IISIEVGDRF ALWDLDWQIP
110 120 130 140 150
QQYGIQQVYG ENGGPGGLFH SLRIIPPILD ICADVADICP DAWIFNYSNP
160 170 180 190 200
MSRICTTVHR RFPELNFVGM CHEIASLERY LPEMLNTSFD NLSLRAGGLN
210 220 230 240 250
HFSVLLDARY KDSGKDAYAD VRAKAPDYFA SLPGYSDILA YTRQHGKLVD
260 270 280 290 300
TEGSTERHAL GGKDSSYPWA DRTLFKEILE KFHCMPITVD SHFGEYISWA
310 320 330 340 350
GEVSDHRGIL DFYTFYRNYL GGVQPKIELK LKERVVSIME GILTDSGYEE
360 370 380 390 400
AAVNIPNRGF IKQLPEFIAV EVPAIIDRKG VHGIQVDIPP GIGGLLSNQI
410 420 430 440 450
AIHDLTAEAI IAGSRDLVIQ ALLVDSVNNQ CRAIPELVDV MISRQQPWLN

YLK
Length:453
Mass (Da):50,341
Last modified:November 24, 2009 - v2
Checksum:i64B178085AE436AC
GO

Sequence cautioni

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

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279280 Genomic DNA. Translation: AAK28734.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279280 Genomic DNA. Translation: AAK28734.1. Different initiation.

3D structure databases

ProteinModelPortaliQ9AI65.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA01004.
BRENDAi3.2.1.20. 2149.
3.2.1.86. 2149.

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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 55 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.