O06901 (MALH_FUSMR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Maltose-6'-phosphate glucosidase
EC=3.2.1.122

Alternative name(s):
6-phospho-alpha-D-glucosidase

Gene names

Name:

malH

Organism

Fusobacterium mortiferum

Taxonomic identifier

850 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Fusobacteria › Fusobacteriia › Fusobacteriales › Fusobacteriaceae › Fusobacterium

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides including maltose-6'P, trehalose-6P and the 6'-phosphorylated derivatives of the five linkage-isomeric alpha-D-glucosyl-D-fructoses: trehalulose-6'P, turanose-6'P, maltulose-6'P, leucrose-6'P, and palatinose-6'P. However, sucrose-6P is not a substrate for MalH, and this enzyme also fails to hydrolyze beta-O-linked phosphorylated disaccharides such as cellobiose-6'P and gentobiose-6'P.
Catalytic activity	Maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate.
Cofactor	NAD. Divalent metal ion. Manganese, iron, cobalt and nickel ions enhance activity whereas magnesium, zinc, calcium and strontium do not.
Pathway	Glycan degradation; maltose degradation.
Subunit structure	Homotetramer By similarity.
Induction	By the five sucrose isomers and other alpha-glucosides (but not by sucrose or glucose).
Sequence similarities	Belongs to the glycosyl hydrolase 4 family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0-7.5. Temperature dependence: Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Cobalt Iron Manganese Metal-binding NAD Nickel
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	maltose catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	maltose-6'-phosphate glucosidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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		PRO_0000169864
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

Sequences

	Sequence		Length	Mass (Da)
	O06901 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: EE9D85B35FA8AF46	FASTA	441	49,712
	10 20 30 40 50 60 MKQFSILIAG GGSTFTPGII LMLLDNLDKF PIRQIKMFDN DAERQAKIGE ACAILLKEKA 70 80 90 100 110 120 PQIKFSYSTN PEEAFTDIDF VMAHIRVGKY PMRELDEKIP LRHGVVGQET CGPGGIAYGM 130 140 150 160 170 180 RSIGGVIGLI DYMEKYSPNA WMLNYSNPAA IVAEATRRLR PNSKVLNICD MPIGIEVRMA 190 200 210 220 230 240 EILGLESRKD MDIMYYGLNH FGWWKSVRDK QGNDLMPKLR EHVSQYGYVV PKGDNQHTEA 250 260 270 280 290 300 SWNDTFAKAK DVLALDPTTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC 310 320 330 340 350 360 EKVVKNQSSE GCALHIDEHA SYIVDLARAI AFNTKEKMLL IVENNGAIVN FDSTAMVEIP 370 380 390 400 410 420 CIVGSNGPEP LVVGRIPQFQ KGMMEQQVTV EKLTVEAWIE GSYQKLWQAI TMSKTVPSAK 430 440 VAKDILDDLI EANKEYWPVL K

References

[1]	"6-phospho-alpha-D-glucosidase from Fusobacterium mortiferum: cloning, expression, and assignment to family 4 of the glycosylhydrolases." Bouma C.L., Reizer J., Reizer A., Robrish S.A., Thompson J. J. Bacteriol. 179:4129-4137(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25557 / CCUG 14475.
[2]	"Purification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-alpha-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyzes maltose 6-phosphate and related phospho-alpha-D-glucosides." Thompson J., Gentry-Weeks C.R., Nguyen N.Y., Folk J.E., Robrish S.A. J. Bacteriol. 177:2505-2512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32, CHARACTERIZATION. Strain: ATCC 25557 / CCUG 14475.
[3]	"Metabolism of sucrose and its five isomers by Fusobacterium mortiferum." Pikis A., Immel S., Robrish S.A., Thompson J. Microbiology 148:843-852(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE SPECIFICITY. Strain: ATCC 25557 / CCUG 14475.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U81185 Genomic DNA. Translation: AAB63015.1.
3D structure databases
ProteinModelPortal	O06901.
SMR	O06901. Positions 2-440.
ModBase	Search...
Protein family/group databases
CAZy	GH4. Glycoside Hydrolase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.2.1.122. 2369.
UniPathway	UPA00150.
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_FUSMR

Accession

Primary (citable) accession number: O06901

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 1, 1997
Last modified:	May 29, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program