ID A0A0M8V8R5_9ACTN Unreviewed; 474 AA.
AC A0A0M8V8R5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ADL01_31840 {ECO:0000313|EMBL:KOV61061.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV61061.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV61061.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV61061.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOV61061.1}.
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DR EMBL; LGDW01000455; KOV61061.1; -; Genomic_DNA.
DR RefSeq; WP_053745461.1; NZ_LGDW01000455.1.
DR AlphaFoldDB; A0A0M8V8R5; -.
DR PATRIC; fig|1519490.3.peg.6936; -.
DR OrthoDB; 3317993at2; -.
DR Proteomes; UP000037738; 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; -; 1.
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; PF00652; Ricin_B_lectin; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..474
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038748231"
FT DOMAIN 39..165
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 474 AA; 50316 MW; 6EFE9351EA8D1226 CRC64;
MRRRSFSRRH LSVMLAAAVT VLIALAATLV ANPAQAATSG ALRGTGSGRC LDVSGAGQAD
GTLVQIWDCN GATNQQWTST DSNQLTVYGN KCLDVPGHAT TAGTRLQIWG CSGGANQQWR
VNSDGTIVGV ESGLCLAATG SATANGTAVE IGTCNGGSNQ KWTGLSGTTP PPGGPCSLPS
TYRWSSTGAL AQPANGWVSL KDFTNVVYQG KHLVYASNVS GSSYGSMAFK PFTNWSDMAS
AGQTGMSQGT VAPTLFYFAP KNIWVLAYQW GAWPFIYRTS SDPTNPNGWS APQPLFTGSI
PGGAPIDQTL IADGQNMYLF FAGDNGKIYR ASMPLGNFPG NFGSSYTTIM SDTVKNLFEA
PEVYKVQGQN QYLMIVEARG ASEQRFFRSF TATSLNGSWT PQAATESNPF AGKANSGANW
TNDISHGDLV RNNPDQTKTI DPCNLQLLYQ GKSPNANGPY DQLPWRPGVL TLQR
//
