MALH_FUSMR
ID MALH_FUSMR Reviewed; 441 AA.
AC O06901;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Maltose-6'-phosphate glucosidase;
DE EC=3.2.1.122;
DE AltName: Full=6-phospho-alpha-D-glucosidase;
GN Name=malH;
OS Fusobacterium mortiferum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25557 / DSM 19809 / CCUG 14475 / VPI 4123A;
RX PubMed=9209025; DOI=10.1128/jb.179.13.4129-4137.1997;
RA Bouma C.L., Reizer J., Reizer A., Robrish S.A., Thompson J.;
RT "6-phospho-alpha-D-glucosidase from Fusobacterium mortiferum: cloning,
RT expression, and assignment to family 4 of the glycosylhydrolases.";
RL J. Bacteriol. 179:4129-4137(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-32, AND CHARACTERIZATION.
RC STRAIN=ATCC 25557 / DSM 19809 / CCUG 14475 / VPI 4123A;
RX PubMed=7730284; DOI=10.1128/jb.177.9.2505-2512.1995;
RA Thompson J., Gentry-Weeks C.R., Nguyen N.Y., Folk J.E., Robrish S.A.;
RT "Purification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-
RT alpha-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyzes maltose 6-
RT phosphate and related phospho-alpha-D-glucosides.";
RL J. Bacteriol. 177:2505-2512(1995).
RN [3]
RP SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 25557 / DSM 19809 / CCUG 14475 / VPI 4123A;
RX PubMed=11882720; DOI=10.1099/00221287-148-3-843;
RA Pikis A., Immel S., Robrish S.A., Thompson J.;
RT "Metabolism of sucrose and its five isomers by Fusobacterium mortiferum.";
RL Microbiology 148:843-852(2002).
CC -!- FUNCTION: Hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides
CC including maltose-6'P, trehalose-6P and the 6'-phosphorylated
CC derivatives of the five linkage-isomeric alpha-D-glucosyl-D-fructoses:
CC trehalulose-6'P, turanose-6'P, maltulose-6'P, leucrose-6'P, and
CC palatinose-6'P. However, sucrose-6P is not a substrate for MalH, and
CC this enzyme also fails to hydrolyze beta-O-linked phosphorylated
CC disaccharides such as cellobiose-6'P and gentobiose-6'P.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-
CC phosphate; Xref=Rhea:RHEA:20421, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57478, ChEBI:CHEBI:61548; EC=3.2.1.122;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Note=Divalent metal ion. Manganese, iron, cobalt and nickel ions
CC enhance activity whereas magnesium, zinc, calcium and strontium do
CC not.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-7.5.;
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.;
CC -!- PATHWAY: Glycan degradation; maltose degradation.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INDUCTION: By the five sucrose isomers and other alpha-glucosides (but
CC not by sucrose or glucose).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR EMBL; U81185; AAB63015.1; -; Genomic_DNA.
DR RefSeq; WP_005886208.1; NZ_QSTZ01000004.1.
DR AlphaFoldDB; O06901; -.
DR SMR; O06901; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR GeneID; 66568212; -.
DR KEGG; ag:AAB63015; -.
DR BRENDA; 3.2.1.122; 1508.
DR SABIO-RK; O06901; -.
DR UniPathway; UPA00150; -.
DR GO; GO:0050081; F:maltose-6'-phosphate glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0000025; P:maltose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR019802; GlycHydrolase_4_CS.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; PTHR32092; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cobalt; Direct protein sequencing; Glycosidase;
KW Hydrolase; Iron; Manganese; Metal-binding; NAD; Nickel.
FT CHAIN 1..441
FT /note="Maltose-6'-phosphate glucosidase"
FT /id="PRO_0000169864"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 4..70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 109
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 49712 MW; EE9D85B35FA8AF46 CRC64;
MKQFSILIAG GGSTFTPGII LMLLDNLDKF PIRQIKMFDN DAERQAKIGE ACAILLKEKA
PQIKFSYSTN PEEAFTDIDF VMAHIRVGKY PMRELDEKIP LRHGVVGQET CGPGGIAYGM
RSIGGVIGLI DYMEKYSPNA WMLNYSNPAA IVAEATRRLR PNSKVLNICD MPIGIEVRMA
EILGLESRKD MDIMYYGLNH FGWWKSVRDK QGNDLMPKLR EHVSQYGYVV PKGDNQHTEA
SWNDTFAKAK DVLALDPTTL PNTYLKYYLF PDYVVEHSNK EYTRANEVMD GREKFVFGEC
EKVVKNQSSE GCALHIDEHA SYIVDLARAI AFNTKEKMLL IVENNGAIVN FDSTAMVEIP
CIVGSNGPEP LVVGRIPQFQ KGMMEQQVTV EKLTVEAWIE GSYQKLWQAI TMSKTVPSAK
VAKDILDDLI EANKEYWPVL K
