GenomeNet

Database: UniProt
Entry: A0A0F0I7X4_ASPPU
LinkDB: A0A0F0I7X4_ASPPU
Original site: A0A0F0I7X4_ASPPU 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system