ID A0A0F0I7X4_ASPPU Unreviewed; 381 AA.
AC A0A0F0I7X4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 03-MAY-2023, entry version 20.
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=P875_00034413 {ECO:0000313|EMBL:KJK62777.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK62777.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK62777.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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:KJK62777.1}.
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DR EMBL; JZEE01000597; KJK62777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0I7X4; -.
DR STRING; 1403190.A0A0F0I7X4; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000033540; 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|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR026534, ECO:0000313|EMBL:KJK62777.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..381
FT /note="Arabinan endo-1,5-alpha-L-arabinosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002443244"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 171
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 381 AA; 42309 MW; 97BF51A518FE25CE CRC64;
MLRNYIISLA CLLGMVQAAP SDNSKPAHPP NVFSKTDKFP LPNQGHLNVH DPNILQHDNN
FYLFKGGIQV PIFKSSNLSG PWTEIGTVLD GPTIIEKQNR TRPWAPTTVE WKGKFYCFYT
VSQDGARNSA IGVASTDSID NGSWTDHGGL IYTEKGPLAH IWPYTVSNAI DASFIVDQQT
QQPYLLYGSY WHGIFQVPLA DDLLSVKNPE KPDAKNLVYV PDGMPKADEG SFMSYKDPYY
YVWYSHGKCC HFNKGFPAMG QEYSIRVGRS KNVRGPFVDK QGKDLAEGGG TTVYDSNHGI
VYAPGGVGVL AATTTDPEVL YYHYLNTSVG FLHGDALLGW NYLDYEDGWP VARFVPGTLN
VGLILIILWQ RNGELCIYCS T
//