ID A0A2H3IF94_9EURO Unreviewed; 508 AA.
AC A0A2H3IF94;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU367111};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU367111};
GN ORFNames=PENO1_068310 {ECO:0000313|EMBL:PCG96462.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG96462.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG96462.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG96462.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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|ARBA:ARBA00004834, 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:PCG96462.1}.
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DR EMBL; NPFK01000212; PCG96462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IF94; -.
DR STRING; 290292.A0A2H3IF94; -.
DR OrthoDB; 2573673at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000218381; 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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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 Lectin {ECO:0000313|EMBL:PCG96462.1};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU367111};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Secreted {ECO:0000256|RuleBase:RU367111};
KW Signal {ECO:0000256|RuleBase:RU367111};
KW Xylan degradation {ECO:0000256|RuleBase:RU367111}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT CHAIN 27..508
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT /id="PRO_5027151823"
FT DOMAIN 28..344
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 362..503
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 307
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 29..39
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 89..94
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 185..186
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 411..449
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 508 AA; 53026 MW; 051A4C7954B61C60 CRC64;
MLFSRPALER FSSVLALSLY VTGSLAGPCD IYSSGGTPCV AAHSTTRALY DSFTGALYQV
SRGSDGATTD ISPLSAGGVA NAAAQDSFCA STTCLITIIY DQSGNGNHLT QAPPGGAASG
PDANGYDYLA SAIGAPVTLN GSKAYGVFIS PFTGYRNNAA RGTATGDEPE GMYAVLDGTH
YNTGCCFDYG NAEVSSDDTG NGHMEAIYFG TGDGSGRGTG SGSGPWIMAD LENGLFSGYD
PINNNADPTI TSRFVTAIIK GEPNQWAIRG GDATTGSLST YYSGIRPSGG YYPMSKEGAI
ILGTGGDNSD RAQGTFYEGV MTSGYPSDDI ESQVQANIVA AKYATTSLIS GPELEVGENI
ALRATTACCT TRYIAHTGST VNTQVVTSSD SEALRKQATW TVRTGLGNSA CYSFESVDTP
GSFIRHSNYE LMLNANDGSK LFGEDATFCP QSGLNGQGNS FRSWSYPARY WRHYNAIGYI
ASNGGPFDFD STTSFNDDVS FVISVGFA
//
