ID   ABFB_PENCN              Reviewed;         463 AA.
AC   U6BLZ9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Alpha-L-arabinofuranosidase B;
DE            Short=ABF B;
DE            Short=Arabinosidase B;
DE            EC=3.2.1.55;
DE   AltName: Full=Alpha-L-arabinofuranosidase of 60kDa;
DE            Short=AF-60;
DE   Flags: Precursor;
GN   Name=abfB; Synonyms=Abf54A;
OS   Penicillium canescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5083;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SIGNAL SEQUENCE CLEAVAGE SITE, SUBCELLULAR
RP   LOCATION, GLYCOSYLATION AT ASN-280, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=24211368; DOI=10.1016/j.carres.2013.08.026;
RA   Gusakov A.V., Sinitsyna O.A., Rozhkova A.M., Sinitsyn A.P.;
RT   "N-glycosylation patterns in two alpha-l-arabinofuranosidases from
RT   Penicillium canescens belonging to the glycoside hydrolase families 51 and
RT   54.";
RL   Carbohydr. Res. 382:71-76(2013).
RN   [2]
RP   SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=14640962; DOI=10.1023/b:biry.0000009134.48246.7e;
RA   Sinitsyna O.A., Bukhtoyarov F.E., Gusakov A.V., Okunev O.N.,
RA   Bekkarevitch A.O., Vinetsky Y.P., Sinitsyn A.P.;
RT   "Isolation and properties of major components of Penicillium canescens
RT   extracellular enzyme complex.";
RL   Biochemistry (Mosc.) 68:1200-1209(2003).
CC   -!- FUNCTION: Secreted alpha-L-arabinofuranosidase that actively hydrolyzes
CC       p-NP-alpha-L-arabinofuranoside and is specific for furanose
CC       configuration of the carbohydrate ring. Exhibits also significant
CC       activity against polymeric arabinose-containing substrates such as
CC       arabinan and arabinoxylan, a major component of plant hemicellulose.
CC       {ECO:0000269|PubMed:14640962}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC         Evidence={ECO:0000269|PubMed:14640962};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.7. {ECO:0000269|PubMed:14640962};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius. 50 perscent maximal
CC         activity is exhibited at 75 degrees Celsius. Reaction time was 10
CC         min. {ECO:0000269|PubMed:14640962};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14640962,
CC       ECO:0000269|PubMed:24211368}.
CC   -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and
CC       a C-terminal arabinose-binding domain (ABD). {ECO:0000250}.
CC   -!- PTM: Residue Asn-280 is mannosylated with up to 7 mannose residues.
CC       {ECO:0000269|PubMed:24211368}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family. {ECO:0000305}.
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DR   EMBL; KF478992; AHA36630.1; -; mRNA.
DR   AlphaFoldDB; U6BLZ9; -.
DR   SMR; U6BLZ9; -.
DR   CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR   CAZy; GH54; Glycoside Hydrolase Family 54.
DR   iPTMnet; U6BLZ9; -.
DR   UniPathway; UPA00667; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR   InterPro; IPR038964; ABFB.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR39447; PTHR39447; 2.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF09206; ArabFuran-catal; 1.
DR   SUPFAM; SSF110221; SSF110221; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:24211368"
FT   CHAIN           27..463
FT                   /note="Alpha-L-arabinofuranosidase B"
FT                   /id="PRO_0000426724"
FT   REGION          27..308
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          309..463
FT                   /note="ABD"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        229
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         430
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         433
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         453
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   SITE            184..185
FT                   /note="Cis-peptide bond"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:24211368"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..39
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   DISULFID        89..94
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   DISULFID        184..185
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   DISULFID        366..404
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
SQ   SEQUENCE   463 AA;  48630 MW;  3CDD1DBD4B1847B0 CRC64;
     MIPQLNRNYA WAIALGLVAR SSLVSAGPCD IYASGGTPCV AAHGTTRALH DSYTGPLYQV
     KRGSDGATTD IAPRHAGGVA NATHQDTFCA GTTCLITIIY DQSGHGNHLS QAPPGHFIGP
     DSQGYDNLAS AIGAPVTLNG QKAYGVFISP GTGYRNNAAK NTATGDEAEG LYAVLDGTHY
     NNGCCFDYGN AEVSGDDTGN GHMEAIYFGD LTAYGTGSGS GPWIMADLEN GLFSGFNAKN
     NAEDPSLSYR FISAAVKGGP NKWAIRGGNA ASGPLSTFYN GSRPNARGYN PMSKEGAIIL
     GIGGHNSKLT VGSSISLRAT TLCCTTRYVA HNGSTVNTQV VSSSSSAALK QQASWRVRTG
     LANSECFSFE SVDTPNSFLM HNNFVLLLKS NDGTKALHEA ATFCPQLGLN GKGNSIRSWS
     YPTRYFRHYD NVLYAASNGG VHKFDNPASF NDDVSWVVSA SFA