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Q97LM4

- MALH_CLOAB

UniProt

Q97LM4 - MALH_CLOAB

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Protein
Maltose-6'-phosphate glucosidase MalH
Gene
malH, CA_C0533
Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed - 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

Binds 1 NAD per subunit.
Binds 1 manganese 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'P
  3. KM=0.82 mM for turanose-6'P
  4. KM=1.11 mM for maltulose-6'P
  5. KM=1.87 mM for leucrose-6'P
  6. KM=2.47 mM for palatinose-6'P
  7. 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931Substrate By similarity
Sitei109 – 1091Increases basicity of active site Tyr By similarity
Binding sitei147 – 1471Substrate By similarity
Metal bindingi169 – 1691Manganese By similarity
Active sitei170 – 1701Proton donor By similarity
Metal bindingi200 – 2001Manganese By similarity
Active sitei264 – 2641Proton acceptor By similarity
Binding sitei284 – 2841Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 7067NAD By similarity
Add
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. carbohydrate metabolic process Source: UniProtKB-KW
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.
BRENDAi3.2.1.122. 1452.
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: 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 MalH
PRO_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.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1486.
HOGENOMiHOG000239810.
KOiK01232.
OMAiVLAHIRV.
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

MKKFSVVIAG GGSTFTPGIV LMLLDNMDKF PIRKLKFYDN DKERQAIVAG    50
ACEIILKEKA PEIEFLATTN PKEAFTDVDF VMAHIRVGKY AMRELDEKIP 100
LKYGVVGQET CGPGGIAYGM RSIGGVIEIL DYMEKYSPNA WMLNYSNPAA 150
IVAEATRKLR PNSKILNICD MPIGIETRMA EILGLESRKE MTVKYYGLNH 200
FGWWSDIRDK DGNDLMPKLK EHVKKYGYVA ENGDTQHTDA SWNDTFAKAK 250
DVYAVDPSTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC 300
KKVIENQSTK GCKMEIDEHA SYIVDLARAI SYNTHERMLL IVPNNGSIEN 350
FDSTGMVEIP CIVGSNGPEP LTMGKIPQFQ KGLMEQQVSV EKLVVEAWKE 400
KSYQKLWQAI TLSRTVPSAK VAKQILDELI EVNKDYWPEL N 441
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF290982 Genomic DNA. Translation: AAK69556.1 .
AE001437 Genomic DNA. Translation: AAK78512.1 .
PIRi E96965.
RefSeqi NP_347172.1. NC_003030.1.
WP_010963854.1. NC_003030.1.

3D structure databases

ProteinModelPortali Q97LM4.
SMRi Q97LM4. Positions 2-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272562.CA_C0533.

Protein family/group databases

CAZyi GH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK78512 ; AAK78512 ; CA_C0533 .
GeneIDi 1116716.
KEGGi cac:CA_C0533.
PATRICi 32035429. VBICloAce74127_0736.

Phylogenomic databases

eggNOGi COG1486.
HOGENOMi HOG000239810.
KOi K01232.
OMAi VLAHIRV.
OrthoDBi EOG632D2X.

Enzyme and pathway databases

BioCyci CACE272562:GJIH-574-MONOMER.
BRENDAi 3.2.1.122. 1452.
SABIO-RK Q97LM4.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProi 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 ]
Pfami PF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view ]
PRINTSi PR00732. GLHYDRLASE4.
SUPFAMi SSF56327. SSF56327. 1 hit.
PROSITEi PS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 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

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

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