ID   APY_BIFLN               Reviewed;         757 AA.
AC   E7CY69;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Exo-alpha-(1->6)-L-arabinopyranosidase;
DE            Short=APY;
DE            EC=3.2.1.-;
DE   AltName: Full=Beta-D-galactopyranosidase;
GN   Name=apy;
OS   Bifidobacterium longum.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=216816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RC   STRAIN=H-1;
RX   PubMed=21851513; DOI=10.1111/j.1365-2672.2011.05128.x;
RA   Lee J.H., Hyun Y.J., Kim D.H.;
RT   "Cloning and characterization of alpha-L-arabinofuranosidase and
RT   bifunctional alpha-L-arabinopyranosidase/beta-D-galactopyranosidase from
RT   Bifidobacterium longum H-1.";
RL   J. Appl. Microbiol. 111:1097-1107(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of a non-reducing terminal alpha-L-
CC       arabinopyranosidic linkage in ginsenoside Rb2 (alpha-L-
CC       arabinopyranosyl-(1->6)-alpha-D-glucopyranosyl) to release alpha-D-
CC       glucopyranosyl (Rd). It is not able to hydrolyze alpha-L-
CC       arabinofuranosyl-(1->6)-alpha-D-glucopyranosyl (Rc).
CC       {ECO:0000269|PubMed:21851513}.
CC   -!- ACTIVITY REGULATION: Completely inhibited by Cu(2+) and activated by
CC       Co(2+). {ECO:0000269|PubMed:21851513}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.24 mM for p-nitrophenyl-alpha-L-arabinopyranoside (pNP-aL-Ap)
CC         {ECO:0000269|PubMed:21851513};
CC         KM=0.26 mM for p-nitrophenyl-beta-D-galactopyranoside (pNP-bD-Ga)
CC         {ECO:0000269|PubMed:21851513};
CC         KM=1.33 mM for Rb2 {ECO:0000269|PubMed:21851513};
CC         Vmax=0.21 umol/min/mg enzyme with Rb2 as substrate
CC         {ECO:0000269|PubMed:21851513};
CC         Vmax=10.02 umol/min/mg enzyme with pNP-aL-Ap as substrate
CC         {ECO:0000269|PubMed:21851513};
CC         Vmax=16.5 umol/min/mg enzyme with pNP-bD-Ga as substrate
CC         {ECO:0000269|PubMed:21851513};
CC       pH dependence:
CC         Optimum pH is 6.8. {ECO:0000269|PubMed:21851513};
CC       Temperature dependence:
CC         Optimum temperature is 48 degrees Celsius.
CC         {ECO:0000269|PubMed:21851513};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; HM803112; ADT80794.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7CY69; -.
DR   SMR; E7CY69; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   eggNOG; COG1472; Bacteria.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase.
FT   CHAIN           1..757
FT                   /note="Exo-alpha-(1->6)-L-arabinopyranosidase"
FT                   /id="PRO_0000422132"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   757 AA;  81473 MW;  D30956BDB329A3FE CRC64;
     MSESTYPSVK DLTLEEKASL TSGGDAWHLQ GVESKGIPSY MITDGPHGLR KSLASSAGET
     DLDDSVPATC FPPAAGLSSS WNPELIHKVG EAMAEECIQE KVAVILGPGV NIKRNPLGGR
     CFEYWSEDPY LAGHEAIGIV EGVQSKGVGT SLKHFAANNQ ETDRLRVDAR ISPRALREIY
     FPAFEHIVKK AQPWTIMCSY NRINGVHSAQ NHWLLTDVLR DEWGFDGIVM SDWGADHDRG
     ASLNAGLNLE MPPSYTDDQI VYAVRDGLIT PAQLDRMAQG MIDLVNKTRA AMSIDNYRFD
     VDAHDEVAHQ AAIESIVMLK NDDAILPLNA GPVANPSATP QKIAVIGEFA RTPRYQGGGS
     SHITPTKMTS FLDTLAERGI KADFAPGFTL DLEPADPALE SEAVETAKNA DVVLMFLGLP
     EAVESEGFDR DTLDMPAKQI ALLEQVAAAN QNVVVVLSNG SVITVAPWAK NAKGILESWL
     LGQSGGPALA DVIFGQVSPS GKLAQSIPLD INDDPSMLNW PGEEGHVDYG EGVFAGYRYY
     DTYGKAVDYP FGYGLSYATF EITGVAVAKT GANTATVTAT VTNTSDVDAA ETVQVYVVPG
     KADVARPKHE LKGFTKAFLK AGESKTVAID LDERAFAYWS EKYNDWHVEA GEYAIEVGVS
     SRDIADTVAV ALDGDGKTQP LTEWSTYGEW EADPFGAKIV AAVAAAGEAG ELTKLPDNAM
     MRMFLNPMPI NSLPTLLGEG GKKIAQFMLD EYAKLSK