Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q97LM4 (MALH_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:malH
Ordered Locus Names:CA_C0533
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 NAD per subunit.

Binds 1 manganese ion per subunit.

Subunit structure

Homotetramer.

Induction

By maltose and other alpha-glucosides, except sucrose.

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

Biophysicochemical properties

Kinetic parameters:

KM=28.4 µM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate Ref.3

KM=1.92 mM for trehalulose-6'P

KM=0.82 mM for turanose-6'P

KM=1.11 mM for maltulose-6'P

KM=1.87 mM for leucrose-6'P

KM=2.47 mM for palatinose-6'P

KM=1.95 mM for maltose-6'P

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

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

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

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

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

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

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

Mass spectrometry

Molecular mass is 49973 Da from positions 1 - 441. Determined by ESI. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Maltose-6'-phosphate glucosidase MalH
PRO_0000169863

Regions

Nucleotide binding4 – 7067NAD By similarity

Sites

Active site1701Proton donor By similarity
Active site2641Proton acceptor By similarity
Metal binding1691Manganese By similarity
Metal binding2001Manganese By similarity
Binding site931Substrate By similarity
Binding site1471Substrate By similarity
Binding site2841Substrate By similarity
Site1091Increases basicity of active site Tyr By similarity

Experimental info

Mutagenesis1691C → S: Loss of activity. Ref.3
Mutagenesis1701D → N: Loss of activity. Ref.3
Mutagenesis1711M → V: Highly reduced activity. Ref.3
Mutagenesis1721P → A: Reduced activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q97LM4 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: B525EE15EC0CD69E

FASTA44149,972
        10         20         30         40         50         60 
MKKFSVVIAG GGSTFTPGIV LMLLDNMDKF PIRKLKFYDN DKERQAIVAG ACEIILKEKA 

        70         80         90        100        110        120 
PEIEFLATTN PKEAFTDVDF VMAHIRVGKY AMRELDEKIP LKYGVVGQET CGPGGIAYGM 

       130        140        150        160        170        180 
RSIGGVIEIL DYMEKYSPNA WMLNYSNPAA IVAEATRKLR PNSKILNICD MPIGIETRMA 

       190        200        210        220        230        240 
EILGLESRKE MTVKYYGLNH FGWWSDIRDK DGNDLMPKLK EHVKKYGYVA ENGDTQHTDA 

       250        260        270        280        290        300 
SWNDTFAKAK DVYAVDPSTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC 

       310        320        330        340        350        360 
KKVIENQSTK GCKMEIDEHA SYIVDLARAI SYNTHERMLL IVPNNGSIEN FDSTGMVEIP 

       370        380        390        400        410        420 
CIVGSNGPEP LTMGKIPQFQ KGLMEQQVSV EKLVVEAWKE KSYQKLWQAI TLSRTVPSAK 

       430        440 
VAKQILDELI EVNKDYWPEL N 

« Hide

References

« Hide 'large scale' references
[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]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF290982 Genomic DNA. Translation: AAK69556.1.
AE001437 Genomic DNA. Translation: AAK78512.1.
PIRE96965.
RefSeqNP_347172.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97LM4.
SMRQ97LM4. Positions 2-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C0533.

Protein family/group databases

CAZyGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK78512; AAK78512; CA_C0533.
GeneID1116716.
KEGGcac:CA_C0533.
PATRIC32035429. VBICloAce74127_0736.

Phylogenomic databases

eggNOGCOG1486.
HOGENOMHOG000239810.
KOK01232.
OMAVLAHIRV.
OrthoDBEOG632D2X.

Enzyme and pathway databases

BioCycCACE272562:GJIH-574-MONOMER.
BRENDA3.2.1.122. 1452.
SABIO-RKQ97LM4.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR019802. 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]
PfamPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
SUPFAMSSF56327. SSF56327. 1 hit.
PROSITEPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMALH_CLOAB
AccessionPrimary (citable) accession number: Q97LM4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries