ID   16ABF_BIFLN             Reviewed;         522 AA.
AC   E7CY70;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Exo-alpha-(1->6)-L-arabinofuranosidase;
DE            Short=ABF;
DE            EC=3.2.1.-;
GN   Name=afuB;
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, 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       arabinofuranosidic linkage in ginsenoside Rc (alpha-L-arabinofuranosyl-
CC       (1->6)-alpha-D-glucopyranosyl) to release alpha-D-glucopyranosyl (Rd).
CC       It is not able to hydrolyze alpha-L-arabinopyranosyl-(1->6)-alpha-D-
CC       glucopyranosyl (Rb2). {ECO:0000269|PubMed:21851513}.
CC   -!- ACTIVITY REGULATION: Completely inhibited by Cu(2+) and partially
CC       inhibited by Co(2+) and Ba(2+). {ECO:0000269|PubMed:21851513}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.21 mM for p-nitrophenyl-a-l-arabinofuranoside (pNP-aL-Af),
CC         {ECO:0000269|PubMed:21851513};
CC         KM=1.73 mM for Rc {ECO:0000269|PubMed:21851513};
CC         Vmax=32.19 umol/min/mg enzyme with Rc as substrate
CC         {ECO:0000269|PubMed:21851513};
CC         Vmax=71.11 umol/min/mg enzyme with pNP-aL-Af as substrate
CC         {ECO:0000269|PubMed:21851513};
CC       pH dependence:
CC         Optimum pH is 4.7. {ECO:0000269|PubMed:21851513};
CC       Temperature dependence:
CC         Optimum temperature is 57 degrees Celsius.
CC         {ECO:0000269|PubMed:21851513};
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; HM803113; ADT80795.1; -; Genomic_DNA.
DR   RefSeq; WP_008783615.1; NZ_WOWU01000001.1.
DR   AlphaFoldDB; E7CY70; -.
DR   SMR; E7CY70; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   eggNOG; COG3534; Bacteria.
DR   OMA; SKYMRGW; -.
DR   BRENDA; 3.2.1.55; 851.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase.
FT   CHAIN           1..522
FT                   /note="Exo-alpha-(1->6)-L-arabinofuranosidase"
FT                   /id="PRO_0000422140"
FT   ACT_SITE        186
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        310
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            314
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            370
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   522 AA;  57431 MW;  BDCD65473F36B578 CRC64;
     MSEHSHDNKP GELEESRLVV DNDFEVAPVN DRLFGSFVEH LGRCVYDGIY EPGHPEADED
     GFRKDVIELV KELGATTIRY PGGNFVSGYR WEDGVGPRDE RPRRLDLAWH STETNQFGLH
     EMAKWLEKTG GNELMEAVNL GTRGLEEALD LLEYANIPGG TKLSEERRAN GADQPFGIKM
     WCLGNEMDGP WQTGHKSAED YGTLAASVAA GMRAIDPNVE LVVCGSSSHV MDTFGKWEET
     VLEKTFDNVN FVSCHAYYHP ELQPDGTRDM KSFLASGVDM DGFINDVAAA IDATKARLKS
     KHDVFISFDE WNVWYLNEEP SKNPEGIGNW PVAPRLLEDV YSAADAVVFG DLMITLLKNA
     DRVHAASLAQ LVNVIAPIMT EPGGPAWRQT TFYPFSLTAK LAKGGTVLEP KLASGTYETD
     KYGEVPTINS VAVRGEDGTI SVFVVNRSME AANDFAIKLP EGFALSAVEA QTLHEDDLLA
     KNTLEDQNRV VLHPNTTITS DADTGTVRVT LPPVSWTAVH VK