ID A0A067P312_PLEOS Unreviewed; 390 AA.
AC A0A067P312;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU368117};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU368117};
GN ORFNames=PLEOSDRAFT_152719 {ECO:0000313|EMBL:KDQ33635.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ33635.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. Releases L-arabinose from arabinoxylan.
CC {ECO:0000256|ARBA:ARBA00025637, ECO:0000256|RuleBase:RU368117}.
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:0000256|ARBA:ARBA00001462,
CC ECO:0000256|RuleBase:RU368117};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU368117}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family.
CC {ECO:0000256|ARBA:ARBA00007396, ECO:0000256|RuleBase:RU368117}.
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DR EMBL; KL198004; KDQ33635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067P312; -.
DR STRING; 1137138.A0A067P312; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_152719; -.
DR HOGENOM; CLU_041805_0_1_1; -.
DR InParanoid; A0A067P312; -.
DR OrthoDB; 1772551at2759; -.
DR Proteomes; UP000027073; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd08987; GH62; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR40631:SF2; ALPHA-L-ARABINOFURANOSIDASE; 1.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU368117};
KW Hydrolase {ECO:0000256|RuleBase:RU368117, ECO:0000313|EMBL:KDQ33635.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368117};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368117}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..390
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001647209"
FT DOMAIN 17..52
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 390 AA; 41991 MW; E73455F1DCD44072 CRC64;
MHQAFVFLTA LASAALAAVP LYGQCGGSGW AGETTCTTGI CSIQNEWYSQ CIPGQATNPP
ASTVSSTSTA PNPVETTLPS SFTWSSSGIL ISPRVDSRNL SAWKDPSIVF YNGKYHVFAS
TAHDAGYNLV YLSFTDFNEA DAAPFYYLDQ TPIGSGYRAA PQVFLMAPQN KWYLIFQNGN
AAYSTNSDIS NPNGWTPPKN FYSGTPSIIT NNIGSGFWVD MWVICDSSNC HLFSSDDNGH
LYRSQTSVSN FPAGMSEPVI ALQDSNSHNL FEASNVYKVG DGFLLVVECI GSNGHRYFRS
WSGASLSGSW TPLAASQTNP FAGSANVAFS GTPWTMDISH GEVVRTNVDQ TMSISACGMR
YLYQGVSPTA SGSYNSLPWR LALLTQTSPC
//
