ID A0A1Z5TI78_HORWE Unreviewed; 503 AA.
AC A0A1Z5TI78;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU367111};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU367111};
GN ORFNames=BTJ68_06608 {ECO:0000313|EMBL:OTA35734.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA35734.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA35734.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA35734.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:RU367111};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|RuleBase:RU367111}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367111}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family.
CC {ECO:0000256|ARBA:ARBA00006963, ECO:0000256|RuleBase:RU367111}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTA35734.1}.
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DR EMBL; MUNK01000040; OTA35734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TI78; -.
DR STRING; 1157616.A0A1Z5TI78; -.
DR VEuPathDB; FungiDB:BTJ68_06608; -.
DR InParanoid; A0A1Z5TI78; -.
DR OrthoDB; 2573673at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000194280; 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:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
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; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367111};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|RuleBase:RU367111};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367111};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU367111};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Secreted {ECO:0000256|RuleBase:RU367111};
KW Signal {ECO:0000256|RuleBase:RU367111};
KW Xylan degradation {ECO:0000256|RuleBase:RU367111}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT CHAIN 23..503
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT /id="PRO_5027151323"
FT DOMAIN 24..339
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 358..498
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 302
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 25..35
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 85..90
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 181..182
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 406..444
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 503 AA; 52309 MW; D902D85949DE6E49 CRC64;
MSPRSSLPYA LGLTTLASLA AAGPCDIYAD GGTPCVAAHS TTRALYDSYQ GPLYQVQRGS
DDATTEITPI SAGGIADASA QDSFCNGTTC LITVIYDQSG TGNDLTRAPP GGAASGPQPN
GYDNLASATG APVTLNGQKA YGVFISPGTG YRNDETTNVA TGDEPEGMYA VFDGTHYNGG
CCFDYGNAET NNLDTGNGHM EALYFGDNTF WGEGSGSGPW IMADLENGLF SGEDPDLNAN
DPTVTYRFLT SSLKGEPNHW AIRGGNAASG GLSTYYDGVR PSVPGYDPMS KEGAILLGIG
GDNSISGQGT FYEGVVTSGY PSDDTEAQVQ ANIVSAGYAT TSLTSGPAVN VGDTVSLHVT
TPGYTGRYLA HSDSDINTQI LTSSSSVSAK QSASWTVTTG LGNSACVSFE SLDVPGSYIR
HYDFVLQLAA DDGSKQMHED ATFCPQAGLT GEGNSITAWG YPTRYIRHFN NEGYVATNGG
PEDFDATRSF NQDVTFLVES ALA
//
