ID   XYLQ_LACPE              Reviewed;         762 AA.
AC   P96793;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Alpha-xylosidase XylQ {ECO:0000303|PubMed:9573180};
DE            EC=3.2.1.177 {ECO:0000269|PubMed:9573180};
GN   Name=xylQ {ECO:0000303|PubMed:9573180};
OS   Lactiplantibacillus pentosus (Lactobacillus pentosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=MD353;
RX   PubMed=9573180; DOI=10.1128/jb.180.9.2312-2320.1998;
RA   Chaillou S., Lokman B.C., Leer R.J., Posthuma C., Postma P.W.,
RA   Pouwels P.H.;
RT   "Cloning, sequence analysis, and characterization of the genes involved in
RT   isoprimeverose metabolism in Lactobacillus pentosus.";
RL   J. Bacteriol. 180:2312-2320(1998).
CC   -!- FUNCTION: Involved in the metabolism of isoprimeverose. Hydrolyzes
CC       isoprimeverose into equimolar amounts of glucose and xylose. In vitro,
CC       can also use p-nitrophenyl-alpha-D-xylopyranoside (alpha-p-NPX).
CC       {ECO:0000269|PubMed:9573180}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues
CC         with release of alpha-D-xylose.; EC=3.2.1.177;
CC         Evidence={ECO:0000269|PubMed:9573180};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 mM for isoprimeverose {ECO:0000269|PubMed:9573180};
CC         KM=1.3 mM for p-nitrophenyl-alpha-D-xylopyranoside
CC         {ECO:0000269|PubMed:9573180};
CC         Vmax=446 nmol/min/mg enzyme with isoprimeverose as substrate
CC         {ECO:0000269|PubMed:9573180};
CC         Vmax=54 nmol/min/mg enzyme with p-nitrophenyl-alpha-D-xylopyranoside
CC         as substrate {ECO:0000269|PubMed:9573180};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9573180};
CC       Peripheral membrane protein {ECO:0000269|PubMed:9573180}; Cytoplasmic
CC       side {ECO:0000269|PubMed:9573180}.
CC   -!- INDUCTION: Expression is negatively regulated by XylR and is subject to
CC       CcpA-dependent catabolite repression. {ECO:0000269|PubMed:9573180}.
CC   -!- DISRUPTION PHENOTYPE: XylP-xylQ double mutant retains the ability to
CC       ferment xylose but is impaired in its ability to ferment
CC       isoprimeverose. {ECO:0000269|PubMed:9573180}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; U89276; AAC62251.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96793; -.
DR   SMR; P96793; -.
DR   STRING; 1589.GCA_001188985_00556; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0061634; F:alpha-D-xyloside xylohydrolase; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.40.1180; -; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR000322; Glyco_hydro_31.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell membrane; Glycosidase; Hydrolase; Membrane.
FT   CHAIN           1..762
FT                   /note="Alpha-xylosidase XylQ"
FT                   /id="PRO_0000440947"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P31434"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000250|UniProtKB:P31434"
SQ   SEQUENCE   762 AA;  86726 MW;  CC09150B72BFBFA9 CRC64;
     MKFTNGYWLN REEYDVNSPK ETYDAQQNGK TITAFAPYTR IMSRGDQLNL GTTTITLTSP
     VENVIGVKLE HFDTNEHGPE FKINNLDPEV AIEVNDQVAS LQSGDLKVTL PLRTDFEMKF
     TANGQLVTQS ETKPQATIWN HDTKVNYMRE QLSMGIDEKI YGLGERFTNF VKNGQVVDTW
     NQDGGTGSEQ AYKNIPFYIS SNGYGVFVDE SQRVSFEIGS ENVDRVQFST EGQSLQYYVI
     YGPTPKEVLH RYTQLTGAIK LPPAWSFGLW LTTSFTTDYS EETVLKFIDG MQEHHIPLDV
     FHFDCFWQKG FEWCTLEWDK EQFPDPEGLL KKIHDRGIKV CVWLNPYIAQ KSPLFKEAKD
     KGYLLTRENG DIWQWDLWQA GNGFVDFTNP AAVKWYQDKL KVLLDMGVDS FKTDFGERIP
     AEDVKFFDGS NPQQEHNYYT LQYNRAVYEV IQQEKGADEA VLFARSQRLV HNPIQYTGAA
     TISRSTAQCV IQLRGGLSFL LSGFGFWSHD IGGFEDGPGT PTADLYKRWS QFGLLSSHSR
     YHGSDVYRVP WNFDDEAVEN TRKYVNKLSL MPYIYTEAAH AAAAYGNPLM RPMFLEFGDD
     DNVYDNATQY MFGSKILVAP IFNDQGKAHF YLPSGKWTSI LDGKVYQAPR TGEWVNEVFD
     ELDLPVLVRQ NSIIVRNEKA VDAAYDYTKD VDIHLYQIQD GNVSSKVVDE HGQDTAEIKV
     ERANGRIVIN TVGLTGDSTV YVHENNDTIK LSLVDGKAEV TL