ID A0A1M2VRW2_TRAPU Unreviewed; 342 AA.
AC A0A1M2VRW2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000256|ARBA:ARBA00012586, ECO:0000256|PIRNR:PIRNR026534};
DE EC=3.2.1.99 {ECO:0000256|ARBA:ARBA00012586, ECO:0000256|PIRNR:PIRNR026534};
GN ORFNames=TRAPUB_13252 {ECO:0000313|EMBL:OJT10232.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT10232.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT10232.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT10232.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000375,
CC ECO:0000256|PIRNR:PIRNR026534};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
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:OJT10232.1}.
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DR EMBL; MNAD01000802; OJT10232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2VRW2; -.
DR STRING; 154538.A0A1M2VRW2; -.
DR OMA; VYGSNHG; -.
DR OrthoDB; 2418563at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000184267; Unassembled WGS sequence.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd18831; GH43_AnAbnA-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW Reference proteome {ECO:0000313|Proteomes:UP000184267};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..342
FT /note="Arabinan endo-1,5-alpha-L-arabinosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012950968"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 152
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:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 342 AA; 36050 MW; 688BD15392F031F5 CRC64;
MIRVAGIPLL LSLLTLALGV LAAFPDPLKL SGSVLIHDPS LVQRASDGKY FLFTTHNKGG
ILTATNLAGP WTSVGSILPS DSSINLPGRD DIWAPDVSLH GSTYYAYYAV STFGSQNSAI
GLATSSSMDP GTWTDQGQVF ASTTGAQFNA IDPNVVIDEK GVPVLSFGSF WSDIFQINLA
SNFKTVSGSA TQVSFNATNP QPEEGAFVWK HGSFYYLFFS SGLCCGFDAN ALPPAGNEYK
VFVGRSTSAH GPFLDKAGKD LRQTGGTLVL ASHGNVYAPG GQSIFTDSKS GKDVFVYHYV
PVNSAQPYSD AFATLGLNAI DWSSVSGFGP VGVGYGNSCV FR
//
