ID A0A179FWX9_METCM Unreviewed; 507 AA.
AC A0A179FWX9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU367111};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU367111};
GN ORFNames=VFPPC_11952 {ECO:0000313|EMBL:OAQ69621.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ69621.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ69621.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ69621.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ69621.1}.
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; LSBJ02000002; OAQ69621.1; -; Genomic_DNA.
DR RefSeq; XP_018146158.1; XM_018289986.1.
DR AlphaFoldDB; A0A179FWX9; -.
DR STRING; 1380566.A0A179FWX9; -.
DR GeneID; 28853980; -.
DR KEGG; pchm:VFPPC_11952; -.
DR OrthoDB; 2573673at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000078397; Chromosome 2.
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:UP000078397};
KW Secreted {ECO:0000256|RuleBase:RU367111};
KW Signal {ECO:0000256|RuleBase:RU367111};
KW Xylan degradation {ECO:0000256|RuleBase:RU367111}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT CHAIN 28..507
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT /id="PRO_5027141246"
FT DOMAIN 29..341
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 360..501
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 304
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 30..40
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 90..95
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 186..187
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 409..448
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 507 AA; 54526 MW; E691ACF7EBFABF25 CRC64;
MSLLDKFSRT VQHACLLLGM YVAASVARPC DIYQSYGTPC VAAHSTTRAL YANYTGELYQ
VKRGSDQATI NITPISAGEV ADAAAQDSFC ARTTCLITII YDQSGHGNHL TQAPPGGAGS
GPEAKGYDSL ASAIGAPVTV HGKKAYGVFI APKTGYRNNK AKHTATGDQA QGMYAVLDGT
HYSTFCCFDY GNAERDNKDT GGGKMEAIYF GIGGFHGSGR GPWVQADLED GMFAGHDHGR
NHKNPSMTSR FVTAVVKGKA GRFAIRGGDG ASGTLSTFYN GKRPNGMYAK MRREGAIVLG
IGGDNSNRGQ GTFYEGAMTK GYPSDKAEAK VQEDIVKAAK YATTSLISGP PFVVGSRVSL
RVTTPCCNTR YIAHSGATMK TQVVSSKSSQ QLKKEASWIV RGGLGFDGCF SFESVDSPGH
FIRLDHNYRL ELAANNGKKL FHETATFCPE AGLYGQGSSL RSWAYPARYW RHFNNDLYAA
SNGNPYYFDA HWRFNEDVSF VAAKSFA
//
