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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • NAD(+)Note: Binds 1 NAD(+) per subunit.
  • Mn2+Note: Binds 1 Mn2+ 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
  1. Vmax=5.2 µmol/min/mg enzyme with p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate as substrate1 Publication
  2. Vmax=0.43 µmol/min/mg enzyme with trehalulose-6'P as substrate1 Publication
  3. Vmax=0.82 µmol/min/mg enzyme with turanose-6'P as substrate1 Publication
  4. Vmax=0.65 µmol/min/mg enzyme with maltulose-6'P as substrate1 Publication
  5. Vmax=0.12 µmol/min/mg enzyme with leucrose-6'P as substrate1 Publication
  6. Vmax=0.60 µmol/min/mg enzyme with palatinose-6'P as substrate1 Publication
  7. 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Manganese, Metal-binding, NAD

Enzyme and pathway databases

BioCyciCACE272562:GJIH-574-MONOMER.
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 Componenti: 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.
OMAiKYPMREK.
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

        10         20         30         40         50
MKKFSVVIAG GGSTFTPGIV LMLLDNMDKF PIRKLKFYDN DKERQAIVAG
60 70 80 90 100
ACEIILKEKA PEIEFLATTN PKEAFTDVDF VMAHIRVGKY AMRELDEKIP
110 120 130 140 150
LKYGVVGQET CGPGGIAYGM RSIGGVIEIL DYMEKYSPNA WMLNYSNPAA
160 170 180 190 200
IVAEATRKLR PNSKILNICD MPIGIETRMA EILGLESRKE MTVKYYGLNH
210 220 230 240 250
FGWWSDIRDK DGNDLMPKLK EHVKKYGYVA ENGDTQHTDA SWNDTFAKAK
260 270 280 290 300
DVYAVDPSTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC
310 320 330 340 350
KKVIENQSTK GCKMEIDEHA SYIVDLARAI SYNTHERMLL IVPNNGSIEN
360 370 380 390 400
FDSTGMVEIP CIVGSNGPEP LTMGKIPQFQ KGLMEQQVSV EKLVVEAWKE
410 420 430 440
KSYQKLWQAI TLSRTVPSAK VAKQILDELI EVNKDYWPEL N
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi272562.CA_C0533.

Protein family/group databases

CAZyiGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1486.
HOGENOMiHOG000239810.
KOiK01232.
OMAiKYPMREK.
OrthoDBiEOG632D2X.

Enzyme and pathway databases

BioCyciCACE272562:GJIH-574-MONOMER.
SABIO-RKQ97LM4.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 83 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

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 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.