ID A0A1I4IUE3_9BACI Unreviewed; 320 AA.
AC A0A1I4IUE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Endo-alpha-(1->5)-L-arabinanase {ECO:0000256|PIRNR:PIRNR026534};
DE EC=3.2.1.99 {ECO:0000256|PIRNR:PIRNR026534};
GN ORFNames=SAMN04487943_102288 {ECO:0000313|EMBL:SFL57593.1};
OS Gracilibacillus orientalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=334253 {ECO:0000313|EMBL:SFL57593.1, ECO:0000313|Proteomes:UP000198565};
RN [1] {ECO:0000313|EMBL:SFL57593.1, ECO:0000313|Proteomes:UP000198565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.4250 {ECO:0000313|EMBL:SFL57593.1,
RC ECO:0000313|Proteomes:UP000198565};
RA de Groot N.N.;
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|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; FOTR01000002; SFL57593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4IUE3; -.
DR STRING; 334253.SAMN04487943_102288; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000198565; 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; cd18829; GH43_BsArb43A-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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..320
FT /note="Endo-alpha-(1->5)-L-arabinanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011527159"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 155..158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 175..177
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT SITE 158
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:PIRSR026534-3"
FT SITE 281
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-3"
SQ SEQUENCE 320 AA; 35900 MW; 1B7474FA3677B2EF CRC64;
MIVKNCLKVL LFVLLFLGVS TVSVSAAFWE MEEHPMIHDP SMIKEGDTWW TFGTGEEDGN
GIRVIYSQDG LNWNEAPVVF PEPLSWWSEY VPNHTSAQWA PDIQYYNGRY WLYYSVSSFG
SNQSLIGLLS TDSISSGNWR DDGLVVHSTT SDNFNAIDGD LVIDEYGNPW LSFGSYWSGI
KLTRLDANTM KPTGQLHSIA ARPNHPEGAV EAPNITYKDG YYYLFVSFDK CCSGLDSTYK
VAVGRSTQIT GPYLDKLGQD MLNGGGTIFD SGNDKWVGPG HQDVYNNNVF LRHAYDADSN
GLPRLLINDL YWDSQGWPVY
//
