Q97LM4 (MALH_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	malH
Ordered Locus Names:	CA_C0533

Organism

Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]

Taxonomic identifier

272562 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium acetobutylicum

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence 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	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

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Manganese Metal-binding NAD
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	maltose-6'-phosphate glucosidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 441	441	Maltose-6'-phosphate glucosidase MalH		PRO_0000169863
Regions
	Nucleotide binding	4 – 70	67	NAD By similarity
Sites
	Active site	170	1	Proton donor By similarity
	Active site	264	1	Proton acceptor By similarity
	Metal binding	169	1	Manganese By similarity
	Metal binding	200	1	Manganese By similarity
	Binding site	93	1	Substrate By similarity
	Binding site	147	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Site	109	1	Increases basicity of active site Tyr By similarity
Experimental info
	Mutagenesis	169	1	C → S: Loss of activity. Ref.3
	Mutagenesis	170	1	D → N: Loss of activity. Ref.3
	Mutagenesis	171	1	M → V: Highly reduced activity. Ref.3
	Mutagenesis	172	1	P → A: Reduced activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q97LM4 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: B525EE15EC0CD69E	FASTA	441	49,972
	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

References

	« Hide 'large scale' referencesShow '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.
PIR	E96965.
RefSeq	NP_347172.1. NC_003030.1.
3D structure databases
ProteinModelPortal	Q97LM4.
SMR	Q97LM4. Positions 2-441.
ModBase	Search...
Protein-protein interaction databases
STRING	272562.CA_C0533.
Protein family/group databases
CAZy	GH4. Glycoside Hydrolase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK78512; AAK78512; CA_C0533.
GeneID	1116716.
KEGG	cac:CA_C0533.
PATRIC	32035429. VBICloAce74127_0736.
Phylogenomic databases
eggNOG	COG1486.
HOGENOM	HOG000239810.
KO	K01232.
OMA	GHSSAGE.
ProtClustDB	CLSK880767.
Enzyme and pathway databases
BioCyc	CACE272562:GJIH-574-MONOMER.
BRENDA	3.2.1.122. 1452.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
InterPro	IPR019802. 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]
Pfam	PF02056. Glyco_hydro_4. 1 hit. PF11975. Glyco_hydro_4C. 1 hit. [Graphical view]
PRINTS	PR00732. GLHYDRLASE4.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
PROSITE	PS01324. GLYCOSYL_HYDROL_F4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MALH_CLOAB

Accession

Primary (citable) accession number: Q97LM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program