ID A0A0Q6XB55_9BURK Unreviewed; 507 AA.
AC A0A0Q6XB55;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU368117};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU368117};
GN ORFNames=ASC87_18740 {ECO:0000313|EMBL:KQW00323.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQW00323.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQW00323.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW00323.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW00323.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW00323.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the degradation of xylan and is a key enzyme in
CC the complete degradation of the plant cell wall. It has a specific
CC arabinofuranose-debranching activity on xylan from gramineae. Acts
CC synergistically with the xylanases and binds specifically to xylan.
CC From small arabinoxylo-oligosides (ranging from arabinoxylotriose to
CC arabinoxylohexaose), it liberates arabinose and, after prolonged
CC incubation, the purified enzyme exhibits some xylanolytic activity as
CC well. {ECO:0000256|RuleBase:RU368117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00001462,
CC ECO:0000256|RuleBase:RU368117};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU368117}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family.
CC {ECO:0000256|RuleBase:RU368117}.
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:KQW00323.1}.
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DR EMBL; LMDI01000009; KQW00323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6XB55; -.
DR STRING; 1736433.ASC87_18740; -.
DR Proteomes; UP000051465; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd08987; GH62; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 3.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR40631:SF2; ALPHA-L-ARABINOFURANOSIDASE; 1.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU368117};
KW Hydrolase {ECO:0000256|RuleBase:RU368117};
KW Reference proteome {ECO:0000313|Proteomes:UP000051465};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368117};
KW Signal {ECO:0000256|RuleBase:RU368117, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..507
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006297419"
FT DOMAIN 37..172
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 507 AA; 54993 MW; 0E2393A4F5427310 CRC64;
MRYRFAQSAL AAFALSVGTL MAGASAQAAI TVDSNTWYAV VNVNSGKALD LYNWVTGDGA
EFRQWSRLDG TNQQFQLVNS GNGYYRLKNR HSGKVVDVWN FSKADGAAVN QFTDGDGVNQ
QWRLEGSDNN AVRFINRNSG KALEVANAST ADGGDITQYT DYGGRNQTWA LVPVGTASPP
PTGGAGNVKL PSSFQWSSSA ALMLAKPAAR FPEVAIKDPT VVYYNGLWHV FSTQAKGNGW
GLEHRSFSDW SNAGAATPYF LDATAIGAGY RAAPFVFFHA PSRLWYLVFQ NGNAAYSTNP
DINNPGGWSA LRTFYSSVPP IVQQNISNNR GHWLDFAVAC DSVNCHLFSA GDNGQIYRSQ
TTLGNFPNGF GDTVIALQDA NRDNLFEAPQ VYKVRETGQY LLIVEAIGSS GRYFRSWTAS
SLGGTWTPLA ATESNPFAGN ANVTFPTGKW SQGISHGEIL RTGHDQNVEI SVCNMRFLYQ
GLAPGAKDNY DSLPYRLGLL TQTNSPC
//
