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Protein

Maltose-6'-phosphate glucosidase

Gene

malH

Organism
Fusobacterium mortiferum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Protein has several cofactor binding sites:
  • NAD(+)
  • Mn2+, Fe2+, Co2+, Ni2+Note: Divalent metal ion. Manganese, iron, cobalt and nickel ions enhance activity whereas magnesium, zinc, calcium and strontium do not.

pH dependencei

Optimum pH is 7.0-7.5.

Temperature dependencei

Optimum temperature is 40 degrees Celsius.

Pathwayi

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

  1. maltose-6'-phosphate glucosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

GO - Biological processi

  1. maltose catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Cobalt, Iron, Manganese, Metal-binding, NAD, Nickel

Enzyme and pathway databases

BRENDAi3.2.1.122. 2369.
SABIO-RKO06901.
UniPathwayiUPA00150.

Protein family/group databases

CAZyiGH4. Glycoside Hydrolase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Maltose-6'-phosphate glucosidase (EC:3.2.1.122)
Alternative name(s):
6-phospho-alpha-D-glucosidase
Gene namesi
Name:malH
OrganismiFusobacterium mortiferum
Taxonomic identifieri850 [NCBI]
Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Maltose-6'-phosphate glucosidasePRO_0000169864Add
BLAST

Expressioni

Inductioni

By the five sucrose isomers and other alpha-glucosides (but not by sucrose or glucose).

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO06901.
SMRiO06901. Positions 2-440.
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.
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.

O06901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQFSILIAG GGSTFTPGII LMLLDNLDKF PIRQIKMFDN DAERQAKIGE
60 70 80 90 100
ACAILLKEKA PQIKFSYSTN PEEAFTDIDF VMAHIRVGKY PMRELDEKIP
110 120 130 140 150
LRHGVVGQET CGPGGIAYGM RSIGGVIGLI DYMEKYSPNA WMLNYSNPAA
160 170 180 190 200
IVAEATRRLR PNSKVLNICD MPIGIEVRMA EILGLESRKD MDIMYYGLNH
210 220 230 240 250
FGWWKSVRDK QGNDLMPKLR EHVSQYGYVV PKGDNQHTEA SWNDTFAKAK
260 270 280 290 300
DVLALDPTTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC
310 320 330 340 350
EKVVKNQSSE GCALHIDEHA SYIVDLARAI AFNTKEKMLL IVENNGAIVN
360 370 380 390 400
FDSTAMVEIP CIVGSNGPEP LVVGRIPQFQ KGMMEQQVTV EKLTVEAWIE
410 420 430 440
GSYQKLWQAI TMSKTVPSAK VAKDILDDLI EANKEYWPVL K
Length:441
Mass (Da):49,712
Last modified:July 1, 1997 - v1
Checksum:iEE9D85B35FA8AF46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81185 Genomic DNA. Translation: AAB63015.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81185 Genomic DNA. Translation: AAB63015.1.

3D structure databases

ProteinModelPortaliO06901.
SMRiO06901. Positions 2-440.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00150.
BRENDAi3.2.1.122. 2369.
SABIO-RKO06901.

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

  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.

Entry informationi

Entry nameiMALH_FUSMR
AccessioniPrimary (citable) accession number: O06901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: November 26, 2014
This is version 78 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

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

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.