ID   M9MBT1_PSEA3            Unreviewed;       681 AA.
AC   M9MBT1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE            EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN   ORFNames=PANT_7c00355 {ECO:0000313|EMBL:GAC72953.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC72953.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC       {ECO:0000256|ARBA:ARBA00007186}.
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DR   EMBL; DF196773; GAC72953.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9MBT1; -.
DR   STRING; 1151754.M9MBT1; -.
DR   OrthoDB; 1097767at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31776; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   PANTHER; PTHR31776:SF0; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..681
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004100828"
FT   DOMAIN          484..672
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
FT   REGION          624..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  72708 MW;  42C4E4BA89825FC1 CRC64;
     MKSLSLSWVA LALTMGACSV ASVNAAPSTS AFSSAAVSSP AVTYNVAAKP SRQSKFALAA
     FIETNINSGT DGGLYAETIR NRAFQDNVNN AANTNNALGR GSLLHWTGTS KGTKLTLSLD
     NSLSAALPQS AIVTGQKTDS CGIANSGFEG FSVTKQPYKL AFYARSPTGK PTTVPVEVGL
     YSSDSSKTFA KQTLPLKLSG EWQKFETTLT PSQATSNNNN VFAIKTQGAC NDGFQLNLVS
     LTPPTWQGTV ARPDLAQALA DIKPKYVRLP GGNDLEGNNI PSWFNWTNAV GDLKNRPGRT
     PTWTSDWNTE GLGLMELMDL TEKWGAQAVL GIYAGYSLDG KAVPQNQLGP YIQSALNQLH
     FLLDTTGRWA DLRKSYGRAA PYKFQHVEIG NEDWLGAAVQ TYGPYRWAAF RDAIAKEFPQ
     LTLIASTLLN GVEGAKAVDN HLYATPSQLF AFAEGMDATS RAIPIWELEY ACINNGLTND
     SDIYSGPGRL KHPTLIGALA EATFLAGAER NGDIFYSAAY APLFQNEGTN LTQWTPDLLS
     FNAGQMVKST SYYIQYAWGN HPIEQIHDTS LSTPTNSSHI YHSFGSDGQG HLVAKLINTN
     AEARDVKVQL GTGAKLSATG AKSWQMKGND PQAANTLSNP QAVVPQSSSN GLPPGAQLTS
     DGSLTVTLPA YSATVLNLAL A
//