ID S7ZDQ7_PENO1 Unreviewed; 389 AA.
AC S7ZDQ7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=PDE_01750 {ECO:0000313|EMBL:EPS26811.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26811.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26811.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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}.
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DR EMBL; KB644409; EPS26811.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZDQ7; -.
DR STRING; 933388.S7ZDQ7; -.
DR eggNOG; ENOG502RADR; Eukaryota.
DR HOGENOM; CLU_009397_5_0_1; -.
DR OrthoDB; 2655644at2759; -.
DR PhylomeDB; S7ZDQ7; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000019376; 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:SF5; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE D-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:UP000019376};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..389
FT /note="Arabinan endo-1,5-alpha-L-arabinosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004559857"
FT ACT_SITE 52
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 172
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 389 AA; 43085 MW; 6F0728164741034D CRC64;
MRFYCSILVG ALLAPLVNCQ RSTPSGRPSL PQVYETTITI PLPNEGHLQV HDPNVVLWDN
HYYLFKGGVH IPFFKAASMS GPWTPIGTVL GGDSIIHQGN RSRPWAPTTV ERNGTFYCYY
TLSTSGSRKS AIGVATSTAL DGSPWTDHGA LIRTGDGPGS EVWPFTVTNA IDASFIRDDE
TGTAYLNYGS FWHDIWQVAL TDDWLSIESP AKPNATQLTF VPDETVRPEE GSWMSHHEGY
YYLWFSHGTC CNFEKRGFPH RDQEYSIRVG RSRNVRGPFV DRAGTRLLDG GGTVVYASNH
GLVYAPGGLG ILPGNSSTPD LLYYHYLNTS IGFQDDQAQL GYNYLKYDQG WPVVLEGIVV
QSSAAMMSRL PDMYMTFILG LWMAVLAAL
//