ID   MALEP_LEVBA             Reviewed;         340 AA.
AC   Q03PA4;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Maltose epimerase;
DE            EC=5.1.3.21;
GN   OrderedLocusNames=LVIS_1908;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 /
RC   NCIMB 947 / NCTC 947;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND BIOTECHNOLOGY.
RX   PubMed=24386392; DOI=10.1371/journal.pone.0084508;
RA   Ramkissoon K.R., Miller J.K., Ojha S., Watson D.S., Bomar M.G.,
RA   Galande A.K., Shearer A.G.;
RT   "Rapid identification of sequences for orphan enzymes to power accurate
RT   protein annotation.";
RL   PLoS ONE 8:E84508-E84508(2013).
CC   -!- FUNCTION: Catalyzes the interconversion of alpha and beta anomers of
CC       maltose. {ECO:0000305|PubMed:24386392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-maltose = beta-maltose; Xref=Rhea:RHEA:21228,
CC         ChEBI:CHEBI:18147, ChEBI:CHEBI:18167; EC=5.1.3.21;
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- BIOTECHNOLOGY: Available as a commercial product from Sigma Aldrich
CC       (catalog number M0902). {ECO:0000269|PubMed:24386392}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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DR   EMBL; CP000416; ABJ64968.1; -; Genomic_DNA.
DR   RefSeq; WP_011668589.1; NC_008497.1.
DR   AlphaFoldDB; Q03PA4; -.
DR   SMR; Q03PA4; -.
DR   STRING; 387344.LVIS_1908; -.
DR   KEGG; lbr:LVIS_1908; -.
DR   PATRIC; fig|387344.15.peg.1813; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_1_1_9; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000001652; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0050558; F:maltose epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd09019; galactose_mutarotase_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR015443; Aldose_1-epimerase.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR047215; Galactose_mutarotase-like.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   PANTHER; PTHR10091:SF50; ALDOSE 1-EPIMERASE; 1.
DR   PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF005096; GALM; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..340
FT                   /note="Maltose epimerase"
FT                   /id="PRO_0000425563"
FT   ACT_SITE        178
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        305
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  37356 MW;  0EF17254D3DF6AA8 CRC64;
     MEITKSAAGT LNQQDVSKYV LTNQQGTQVA VLTWGATLQE FSVVEDGKRH SLIVNKPDLA
     GYDHNPYYLC QALGRVAGRI AGAQFELDGQ TVHLEANEEP NASHGGPHGF TFVNWDATTN
     QTADTASVVL THTSTPADDR YPGNLETTIT YTLTEENRLD ITFDAQSDAA TLFNPTIHTY
     FNVTDDQHDL DQQWVKLSGD KRLVLDQAKI PTGEMVPTAG TGYDFSQPRT VKDGLDQLHQ
     TGQVEYDDAF VVEPSKDTPI ATIGDTTGHR EVSIYSDRNG LVVFTANPTD DARADVRDYN
     ALAMEAQTLP DAIHHADFGD VVLPANQPVE HTISYQYTRK
//