ID R1I5R2_9PSEU Unreviewed; 498 AA.
AC R1I5R2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN ORFNames=H480_24817 {ECO:0000313|EMBL:EOD65799.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD65799.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD65799.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD65799.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:EOD65799.1}.
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DR EMBL; AOUO01000371; EOD65799.1; -; Genomic_DNA.
DR AlphaFoldDB; R1I5R2; -.
DR PATRIC; fig|1292037.4.peg.4690; -.
DR eggNOG; COG3693; Bacteria.
DR OrthoDB; 3317993at2; -.
DR Proteomes; UP000014139; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR PANTHER; PTHR40631:SF1; 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 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..48
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 49..498
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004352529"
FT DOMAIN 55..191
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 498 AA; 52926 MW; 4475E8CA260B7530 CRC64;
MSSLGQSPPP GAPRRARRVR PGRALSTLLA TVLATAAAVA LTPAAASAAT VDTNAWYVLV
NRNSGKALDV SGASTADGAA VQQWARHDGA NQQWQFVDSG NGYYRLKSKN SGKVLDVDGW
STADGGKVQQ WTDLNGTNQQ FGLADSDGGY VRLLNRNSGK AVEVSGLSTA DGAAIVQYGD
WQGANQQWQL VRVGDTASCA LPSAYHWSST GSLAEPKAGW GALKDFTNVV YNGKHVVYGS
TTDTSGGYGS MGFAPFTNWS DMASAGQTGM STGTVAPTLF YFAPKNVWIL AYQWGPTTFS
YRTSSDPTNV NGWSAPQELF SGSISGSAPL DQTLIGDGTN MYLFFAGDNG KIYRASMPIG
NFPGSFGSSY TTIMSDTTAN LFEAVEVYQV QGQNQYLMLV EAMGANGRYF RSFTASSLGG
SWTPQAATES NPFAGKANSG ATWTNDISHG DLVRTNPDQT KTVDPCHLQL LYQGRNPASD
GTDYNHLPWR PGVLTLQR
//
