ID A0A124BVR2_ASPNG Unreviewed; 318 AA.
AC A0A124BVR2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ABL_01928 {ECO:0000313|EMBL:GAQ36923.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ36923.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- FUNCTION: Endo-1,5-alpha-L-arabinanase involved in degradation of
CC pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.
CC {ECO:0000256|ARBA:ARBA00025221}.
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:GAQ36923.1}.
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DR EMBL; BCMY01000002; GAQ36923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124BVR2; -.
DR PaxDb; 5061-CADANGAP00002504; -.
DR VEuPathDB; FungiDB:An02g10550; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1144977; -.
DR VEuPathDB; FungiDB:ATCC64974_54210; -.
DR VEuPathDB; FungiDB:M747DRAFT_255051; -.
DR OMA; EDYQFGW; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:SF7; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE C; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..318
FT /note="Arabinan endo-1,5-alpha-L-arabinosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013243916"
FT ACT_SITE 30
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 145
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 318 AA; 34042 MW; A58121E1EF499432 CRC64;
MLSFVLLLCV ALVNAYSDPG ACSGTCWAHD PNVIRRVSDG TYFRFSTGGG IHISSASAIT
GPWTDLGYAL PDGSIVSVGN ASNLWAPDVH YVDGTYYMYY ASSTLGSRSS TIGVATSTTL
EADSWTDHGE IGVTSSSSTP YNAIDPNWIT IGSTPYLQFG SYWQGLYQVE MTDSLTASSS
SPTNLAYNAS GNHAIEASYM YEYGGYYYLT FSSGTAQGYT TSLPAQGDEY RIVVCRSKTG
TGNFVDKDGV SCLNSGGTTV LSSHDYVYGP GGQGIINTTS HGIVVYYHYA DKNIGLAVDE
YQFGWNTLTW TDGWPVVA
//
