ID   MAPP_ENTFT              Reviewed;         274 AA.
AC   E6ENP9;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Maltose 6'-phosphate phosphatase;
DE            Short=Maltose 6'-P phosphatase;
DE            EC=3.1.3.90;
GN   Name=mapP; ORFNames=HMPREF9496_01322;
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, KINETIC PARAMETERS, SUBSTRATE SPECIFICITY,
RP   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 dephosphorylation of intracellular maltose 6'-P
CC       formed during PTS-catalyzed maltose transport, leading to the formation
CC       of maltose. MapP connects PTS-mediated maltose uptake to maltose
CC       phosphorylase-catalyzed metabolism. Is also able to efficiently
CC       dephosphorylate turanose 6'-P, and to a much lesser extent, leucrose
CC       6'-P and maltulose 6'-P. Cannot use glucose 6-P, fructose 6-P and
CC       sucrose 6-P as substrates. {ECO:0000269|PubMed:23490043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-maltose 6'-phosphate + H2O = D-maltose + phosphate;
CC         Xref=Rhea:RHEA:36295, ChEBI:CHEBI:15377, ChEBI:CHEBI:17306,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57478; EC=3.1.3.90;
CC         Evidence={ECO:0000269|PubMed:23490043};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.1 mM for maltose 6'-phosphate {ECO:0000269|PubMed:23490043};
CC         Vmax=25 umol/min/mg enzyme {ECO:0000269|PubMed:23490043};
CC         Note=kcat is 128 sec(-1).;
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow significantly and
CC       reproducibly faster than the wild-type strain on glucose as carbon
CC       source. They are able to transport maltose and grow in maltose-
CC       containing medium, although at significantly slower rate than the wild-
CC       type strain. They seem to accumulate primarily maltose 6'-P when
CC       exposed to a maltose-containing growth medium.
CC       {ECO:0000269|PubMed:23490043}.
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DR   EMBL; AEBB01000034; EFT41761.1; -; Genomic_DNA.
DR   RefSeq; WP_002358863.1; NZ_GL476272.1.
DR   AlphaFoldDB; E6ENP9; -.
DR   SMR; E6ENP9; -.
DR   KEGG; ag:EFT41761; -.
DR   PATRIC; fig|749493.3.peg.1239; -.
DR   HOGENOM; CLU_086635_0_0_9; -.
DR   BRENDA; 3.1.3.90; 2095.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Hydrolase.
FT   CHAIN           1..274
FT                   /note="Maltose 6'-phosphate phosphatase"
FT                   /id="PRO_0000422397"
SQ   SEQUENCE   274 AA;  31205 MW;  EAFC9D4858601793 CRC64;
     MNLLTINTHS WLEEEPLKKL EEIAKVILSS ESEIIALQEV NQKVASKKVP LEQLTTFCPI
     ATQTPIHEDN FAYLIVQYLA EKGQHYYWSW EMSHIGYAIY EEGNALLSKC PLTSEALLIS
     ESQEPTNYRT RKILVAETES SKGTLTVVSG HFSWWETPCT GFAYEWLQLE KYLAMGQQPL
     VILGDLNNPA GTTGYQLVEN SYLPIQDAFV VAEETSGEAT VEKKIDGWEE NEAALRIDYA
     FVPKQWHVRK YEVIFDGRKT PIVSDHFGLL IQLK