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   28-JUN-2023, entry version 106.
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; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   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; 62762379; -.
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   CDD; cd05298; GH4_GlvA_pagL_like; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF14; MALTOSE-6'-PHOSPHATE GLUCOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//