ID M5G5X9_DACPD Unreviewed; 685 AA.
AC M5G5X9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 03-MAY-2023, entry version 36.
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=DACRYDRAFT_104150 {ECO:0000313|EMBL:EJU05666.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU05666.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU05666.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU05666.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH795856; EJU05666.1; -; Genomic_DNA.
DR AlphaFoldDB; M5G5X9; -.
DR STRING; 1858805.M5G5X9; -.
DR HOGENOM; CLU_010060_1_0_1; -.
DR OMA; SVGNQEC; -.
DR OrthoDB; 1097767at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000030653; 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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
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 SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EJU05666.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..685
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004067616"
FT DOMAIN 475..675
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 685 AA; 74954 MW; 0984A2FCFDCA1000 CRC64;
MLGSVLTIWA LALAASANGQ ITPPNALNLR ITQNMTHTIS PTLYLHFLST PVKLLSIVGR
YGYMWEDINH SGDGGLYAEL LQNRALQGVI PNTGAALQGW QSINGAFLTV TAGTSGVSSA
LPNSLQVSIP KTAKGPIRFA NTGYWGINVQ AGWTYTGSLY VKSPGYCGSV TVALQSASGT
IYDSVTLSNV KDTYQKLTFI LSPTNSAPDH NNLFTVTVDG AAAAGQTLYF GMFSLFPPTF
RGRENGLRMD LAQALFDTSP KLWRFPGGNN LEGQTWEQRW KWNETIGPLE NRPGRVGDWG
YPNTDGLGLM EYLDWIEDLE AVPILGVWAG VSIGNYSDLP DWPIVPQDQL QPYIDDVINE
IHFITDPENT SEWAALRAEY GHPAPYNLTY IEVGNEDQFA PDSYQAYRWQ MFVDGINASF
PHLSLQFLAT SPPSLPLDPP YLKIDFHQYS TPGWFINNSY MFDTYPRNGT QWFMGEYAVT
GTETGCELGS PSCGRLLYPT LEGACAEAAF MTGMERNSDV VFASAYAPSL QNVNSYQWTP
DIITFSARSV AKSVSYYNQQ LFATNLGTHV LATIPEPSPS TAPLYWVASH HATNQLVFLK
VVNTGSADLV GNLFFDFPVI GGFGTAQQLS AGLYPTPGVY NISNTLETPD VITPVASSFG
IVDSSEFNYT FPQSSITVMT FAVDF
//
