ID B2WBD2_PYRTR Unreviewed; 501 AA.
AC B2WBD2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU367111};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU367111};
GN ORFNames=PTRG_06944 {ECO:0000313|EMBL:EDU49864.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU49864.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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}.
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DR EMBL; DS231621; EDU49864.1; -; Genomic_DNA.
DR RefSeq; XP_001937277.1; XM_001937242.1.
DR AlphaFoldDB; B2WBD2; -.
DR STRING; 426418.B2WBD2; -.
DR EnsemblFungi; EDU49864; EDU49864; PTRG_06944.
DR GeneID; 6345215; -.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR HOGENOM; CLU_029332_3_0_1; -.
DR InParanoid; B2WBD2; -.
DR OMA; WNYPTRY; -.
DR OrthoDB; 2573673at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000001471; 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:UP000001471};
KW Secreted {ECO:0000256|RuleBase:RU367111};
KW Signal {ECO:0000256|RuleBase:RU367111};
KW Xylan degradation {ECO:0000256|RuleBase:RU367111}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT CHAIN 22..501
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT /id="PRO_5027137927"
FT DOMAIN 23..337
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 356..496
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 300
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 24..34
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 84..89
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 179..180
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 404..442
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 501 AA; 51839 MW; A76136CED365DE8E CRC64;
MSSRSALLAL GVVATSSFVS AGPCDIYASG NTPCIAAHST TRALYNAYSG SLYQVKRGSD
GATTDIKPRS AGGVANAAAQ DTFCASTTCL ISIIYDQSGK GNHLTQAPPG AFKGPDVGGY
DNLAGAIGAP VTLNGQKAYG VFVSPGTGYR NNKVVGSAIG DQSEGMYAVF DGTHFNDGCC
FDYGNAETSN TDTGNGHMEA IYFGSNTIWG SGAGSGPWIM ADLENGLFSG SNPKNNPGDP
TVTSRFLTTV IKGGANKWAI RGGNAASGAL STYYNGARPN ASGYNPMSKE GAIILGIGGD
NSISGQGTFY EGVMTSGYPT DATENAVQQN IVAAKYATTS MTSGPAFTIG SSVSFRATTS
GYTDRYLAHT GATVNTQVVS SSSTALLKRQ ASWTVRAGLA NSACFSFESK DTAGSYIRHY
NFILQLQAND GSKAFKEDAT FCPQAGLTGQ FNTIAAWGYP TRMIRHFNNV GYIASNGGVH
DFDKAASFNA DVTWNVGSSL A
//
