ID   ABFB_MAGO7              Reviewed;         486 AA.
AC   G4MMH2;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Alpha-L-arabinofuranosidase B {ECO:0000305};
DE            EC=3.2.1.55 {ECO:0000269|PubMed:27764242};
DE   AltName: Full=Alpha-N-arabinofuranosidase B {ECO:0000303|PubMed:27764242};
DE   Flags: Precursor;
GN   Name=abfB {ECO:0000303|PubMed:23159799}; ORFNames=MGG_06843;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=23159799; DOI=10.1016/j.jprot.2012.10.029;
RA   Kim S.G., Wang Y., Lee K.H., Park Z.Y., Park J., Wu J., Kwon S.J.,
RA   Lee Y.H., Agrawal G.K., Rakwal R., Kim S.T., Kang K.Y.;
RT   "In-depth insight into in vivo apoplastic secretome of rice-Magnaporthe
RT   oryzae interaction.";
RL   J. Proteomics 78:58-71(2013).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27764242; DOI=10.1371/journal.pone.0165149;
RA   Wu J., Wang Y., Park S.Y., Kim S.G., Yoo J.S., Park S., Gupta R.,
RA   Kang K.Y., Kim S.T.;
RT   "Secreted alpha-N-arabinofuranosidase B protein is required for the full
RT   virulence of Magnaporthe oryzae and triggers host defences.";
RL   PLoS ONE 11:E0165149-E0165149(2016).
CC   -!- FUNCTION: Secreted arabinofuranosidase that causes degradation of rice
CC       cell wall components during infection. Required for virulence.
CC       {ECO:0000269|PubMed:27764242}.
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:27764242};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.206 uM for p-nitrophenyl-alpha-1-arabinofuranoside
CC         {ECO:0000269|PubMed:27764242};
CC         Note=kcat is 0.9148 sec(-1) with p-nitrophenyl-alpha-1-
CC         arabinofuranoside as substrate. {ECO:0000269|PubMed:27764242};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000305|PubMed:27764242}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23159799,
CC       ECO:0000269|PubMed:27764242}. Note=Secreted during fungal infection
CC       into the apoplastic space of host plant (PubMed:23159799,
CC       PubMed:27764242). Only accumulates in rice leaves during compatible
CC       fungal infection (PubMed:27764242). {ECO:0000269|PubMed:23159799,
CC       ECO:0000269|PubMed:27764242}.
CC   -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and
CC       a C-terminal arabinose-binding domain (ABD). {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Significantly reduces vegetative growth and
CC       conidiation, but no difference in germination and appressorium
CC       formation compared to wild-type. Significantly reduces virulence.
CC       {ECO:0000269|PubMed:27764242}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001231; EHA56950.1; -; Genomic_DNA.
DR   RefSeq; XP_003709562.1; XM_003709514.1.
DR   AlphaFoldDB; G4MMH2; -.
DR   SMR; G4MMH2; -.
DR   STRING; 318829.MGG_06843T0; -.
DR   CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   EnsemblFungi; MGG_06843T0; MGG_06843T0; MGG_06843.
DR   GeneID; 2685016; -.
DR   KEGG; mgr:MGG_06843; -.
DR   VEuPathDB; FungiDB:MGG_06843; -.
DR   eggNOG; ENOG502R8XS; Eukaryota.
DR   HOGENOM; CLU_009397_2_1_1; -.
DR   InParanoid; G4MMH2; -.
DR   OMA; HHIWAPE; -.
DR   OrthoDB; 605975at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000009058; Chromosome 1.
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   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF110221; SSF110221; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..486
FT                   /note="Alpha-L-arabinofuranosidase B"
FT                   /id="PRO_5003465844"
FT   REGION          45..342
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   REGION          359..467
FT                   /note="ABD"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q82P90"
FT   ACT_SITE        229
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q82P90"
FT   SITE            166
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q82P90"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   486 AA;  52455 MW;  8BECEC6206713E6F CRC64;
     MLSLKAVLRF ASVAVAVVLP TLAQAQAPEP SLSVRSPPVS YNNTLVKQRA DPQILKHTNG
     RYYFIATVPE YDRVVMRQAD SIQGLSTAEE RLIWARSQSK AGVGYVWAPE LHKIGDKWYI
     YFALGRTAPF DVRPFVLEGT GSDDPMAASW AEKGFITTDF DTFSLDATTF EVNGVRYLSW
     AQADPRFDNG GGTSLFLARM TNPWTIQRPS IVISRPDQPW ERIGHNVNEG SWGMVRNGKV
     FVTYSAAATD ANYCMGLLTA DQNADLMNPA SWSKSKDPVF VSNTATSQFG PGHSAFTVSD
     DNQSDVLVYH ARQYKDIRGE PLDNPDRMTR VQKLYWRSDG TPDFGIPIPD GPHPVRLRSS
     ADQTLYVGIA NNAVQSVKDA PVQNTQFKIV EPGLGGSGTI SFESTAQPGK YLSAANGSVS
     LATLSNTSDA GARSSASFRR VAGLSDATGV SFESAAQAGS YLVSGGNGAA VSVAPSTGAE
     ATFYLE