ID   APY_BIFBA               Reviewed;         757 AA.
AC   F6C6C1;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Exo-alpha-(1->6)-L-arabinopyranosidase;
DE            Short=APY;
DE            EC=3.2.1.-;
GN   OrderedLocusNames=HMPREF9228_1477;
OS   Bifidobacterium breve (strain ACS-071-V-Sch8b).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=866777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-071-V-Sch8b;
RA   Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, AND SUBUNIT.
RC   STRAIN=k-110;
RX   PubMed=14660356; DOI=10.1128/aem.69.12.7116-7123.2003;
RA   Shin H.Y., Park S.Y., Sung J.H., Kim D.H.;
RT   "Purification and characterization of alpha-L-arabinopyranosidase and
RT   alpha-L-arabinofuranosidase from Bifidobacterium breve K-110, a human
RT   intestinal anaerobic bacterium metabolizing ginsenoside Rb2 and Rc.";
RL   Appl. Environ. Microbiol. 69:7116-7123(2003).
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:14660356}.
CC   -!- ACTIVITY REGULATION: Completely inhibited by Cu(2+) and Fe(2+).
CC       {ECO:0000269|PubMed:14660356}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.086 mM for Rb2 (at pH 7 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:14660356};
CC         KM=0.16 mM for p-nitrophenyl-alpha-L-arabinopyranoside (pNP-aL-Ap)
CC         (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:14660356};
CC         Vmax=0.13 umol/min/mg enzyme with Rb2 as substrate (at pH 7 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:14660356};
CC         Vmax=10.7 umol/min/mg enzyme with pNP-aL-Ap as substrate (at pH 7 and
CC         37 degrees Celsius) {ECO:0000269|PubMed:14660356};
CC       pH dependence:
CC         Optimum pH is between 5.5 and 6. {ECO:0000269|PubMed:14660356};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:14660356};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14660356}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; CP002743; AEF27806.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6C6C1; -.
DR   SMR; F6C6C1; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; bbv:HMPREF9228_1477; -.
DR   PATRIC; fig|866777.3.peg.1455; -.
DR   HOGENOM; CLU_004542_4_1_11; -.
DR   OMA; GGRPYNL; -.
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; Hydrolase.
FT   CHAIN           1..757
FT                   /note="Exo-alpha-(1->6)-L-arabinopyranosidase"
FT                   /id="PRO_0000422133"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   757 AA;  81581 MW;  438BA12E0198948A CRC64;
     MSESTYPSVK DLTLEEKASL TSGGDAWHLQ GVESKGIPGY MITDGPHGLR KSLASSAGET
     DLDDSVPATC FPPAAGLSSS WNPELIHKVG EAMAEECIQE KVAVILGPGV NIKRNPLGGR
     CFEYWSEDPY LAGHEAIGIV EGVQSKGVGT SLKHFAANNQ ESDRLRVDAR ISPRALREIY
     FPAFEHIVKK AQPWTIMCSY NRINGVHSAQ NHWLLTDVLR DEWGFEGIVM SDWGADHDRG
     ASLNAGLNLE MPPSYTDDQI VYAVRDGRIT PAQLDRMAQG MIDLVNKTRA AMSIDNYRFD
     VDAHDEVAHQ AAIESIVMLK NDDAILPLNA GPVANPSAMP QKIAVIGEFA RTPRYQGGGS
     SHITPTKMTS FLDTLAERGI KADFAPGFTL DLEPADPALE SEAVETAKNA DVVLMFLGLP
     EAAESEGFDR DTLDMPAKQI TLLEQVAAAN QNVVVVLSNG SVITVAPWAK NAKGILESWL
     LGQSGGPALA DVIFGQVSPS GKLAQSIPLD INDDPSMTNW PGEEGHVDYG EGVFVGYRYY
     DTYGKAVDCP FGYGLSYATF EITGVAVAKT GANTATVNAT VTNTSDVDAA ETVQVYVAPG
     KADVARPKHE LKGFTKVFLK SGESKTVTID LDERAFAYWS EKYNDWHVES GEYAIEVGTS
     SRDIAETVTV ALEGDGKTQP LTEWSTYGEW EADPFGAKIV AAVAAAGEAG ELPKLPDNAM
     MRMFLNSMPI NSLPTLLGEG GKKIAQFMVD EYAKLSK