ID   MALPY_ENTFT             Reviewed;         783 AA.
AC   E6ENP7;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Maltose phosphorylase;
DE            EC=2.4.1.8;
GN   Name=malP; ORFNames=HMPREF9496_01320;
OS   Enterococcus faecalis (strain TX4000 / JH2-2).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=749493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX4000 / JH2-2;
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND DISRUPTION PHENOTYPE.
RC   STRAIN=TX4000 / JH2-2;
RX   PubMed=23490043; DOI=10.1111/mmi.12183;
RA   Mokhtari A., Blancato V.S., Repizo G.D., Henry C., Pikis A., Bourand A.,
RA   de Fatima Alvarez M., Immel S., Mechakra-Maza A., Hartke A., Thompson J.,
RA   Magni C., Deutscher J.;
RT   "Enterococcus faecalis utilizes maltose by connecting two incompatible
RT   metabolic routes via a novel maltose 6'-phosphate phosphatase (MapP).";
RL   Mol. Microbiol. 88:234-253(2013).
CC   -!- FUNCTION: Catalyzes the phosphorolysis of maltose, leading to the
CC       formation of glucose and glucose 1-P. Does not have maltose 6'-P
CC       phosphorylase activity. Plays an important role in the metabolism of
CC       maltose taken up via the bacterial phosphotransferase system (PTS).
CC       {ECO:0000269|PubMed:23490043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose + phosphate = beta-D-glucose 1-phosphate + D-
CC         glucose; Xref=Rhea:RHEA:21116, ChEBI:CHEBI:4167, ChEBI:CHEBI:17306,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57684; EC=2.4.1.8;
CC         Evidence={ECO:0000269|PubMed:23490043};
CC   -!- PATHWAY: Glycan degradation; maltose degradation.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on maltose.
CC       {ECO:0000269|PubMed:23490043}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; AEBB01000034; EFT41759.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ENP7; -.
DR   SMR; E6ENP7; -.
DR   PATRIC; fig|749493.3.peg.1237; -.
DR   HOGENOM; CLU_006285_2_2_9; -.
DR   UniPathway; UPA00150; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0050082; F:maltose phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000025; P:maltose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosyltransferase; Transferase.
FT   CHAIN           1..783
FT                   /note="Maltose phosphorylase"
FT                   /id="PRO_0000422398"
FT   ACT_SITE        507
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         378..379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         610..611
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ   SEQUENCE   783 AA;  90212 MW;  28E0E0E91B46F478 CRC64;
     MQSVAFMIDL SIKSLRGILM KQIKRLFQID PWKIRTTHLD KENLRLQESL TSIGNGYMGM
     RGNFEEHYSG DHHQGTYLAG VWYPDKTRVG WWKNGYPEYF GKVINAINFI AMDLQIDGQT
     IDLATTPYED FSLELDMQNG VLSRQFTIQT PKNKVRFSFE RFLSLEKKEA AYIHLTIEML
     EGTGTITLHS KLDGDVQNED SNYEEHFWEE IAIETQETLG FVTTKTIPNN FEIERFTVTA
     GMRHFIDGAS VVPTYTQQPL ALTAELTVSL NEGETTAITK EVLVVTSRDV PETQQITRVN
     ELFSEMTTLY PEAKAGQAAA WAKRWQLADV VIEGDDEAQQ GIRFNLFQLF STYYGEDDRL
     NIGPKGFTGE KYGGATYWDT EAYAVPLYLA LAKPEVTKNL LKYRHNQLPQ AIHNAQQQGL
     KGALYPMVTF TGVECHNEWE ITFEEIHRNG AIAYAIYNYV NYTGDQDYLK DAGLEVLVAI
     ARFWADRVHF SQRHKQYMIH GVTGPNEYEN NINNNWYTNT IAAWVLRYTR ESYLKFQEET
     TLKIADDELA KWADIVENMY FPVDNELGIF VQHDTFLDKD LMPVSDLPLS ELPLNQHWSW
     DKILRSCFIK QADVLQGIYF FNDAFSLEEK RRNFNFYEPM TVHESSLSPS IHAVLAAELG
     MEEKAVEMYQ RTARLDLDNY NNDTEDGLHI TSMTGSWLAI VQGFAQMKTD HQQLKFAPFL
     PATWTAYSFH INYRNRLLFV EVAADQVAFT LLDGPAIPLT VYDQKYTLKD RLVLPIRKEE
     VHV