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Database: UniProt
Entry: A0A1A5PG45_9ACTN
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ID   A0A1A5PG45_9ACTN        Unreviewed;       488 AA.
AC   A0A1A5PG45;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=A4U61_00810 {ECO:0000313|EMBL:OBQ54370.1};
OS   Streptomyces sp. H-KF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1727216 {ECO:0000313|EMBL:OBQ54370.1, ECO:0000313|Proteomes:UP000093719};
RN   [1] {ECO:0000313|Proteomes:UP000093719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-KF8 {ECO:0000313|Proteomes:UP000093719};
RA   Undabarrena A., Ugalde J.A., Seeger M., Camara B.;
RL   Submitted (APR-2016) 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:OBQ54370.1}.
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DR   EMBL; LWAB01000001; OBQ54370.1; -; Genomic_DNA.
DR   RefSeq; WP_065000177.1; NZ_LWAB01000001.1.
DR   AlphaFoldDB; A0A1A5PG45; -.
DR   OrthoDB; 3317993at2; -.
DR   Proteomes; UP000093719; 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   Reference proteome {ECO:0000313|Proteomes:UP000093719};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..488
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008334377"
FT   DOMAIN          42..178
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   488 AA;  53269 MW;  A5AC2609D230A26F CRC64;
     MWFRHPSPVR PRRLLGVLAP LLLVATFLGA QPAEAATVDP NASYVLVNRN SGKALDVHNL
     ATDDGARITQ WTRNDQNQQQ WQFVDSGGGY YRIKSRHSGK VLDIHNWSTA NGGPIVQWAD
     LNGTNQQWRL ADSSDGYVRL ISRHSNKALE VQGASTADNA NIVQYDDWGG TNQQWQLVKT
     GADTPGACAL PSAYRWTSTG ALAQPKQGWV SLKDFTVAPY NGRQLVYATT HDTGTRWGSM
     NFGLFTNWSE MASAGQNAMS QSTVAPTLFY FAPKNIWVLA YQWGGTAFSY RTSSDPTNPN
     GWSSEQVLFS GSISGSGTGP IDQTLIGDGT NMYLFFAGDN GRIYRASMPI GNFPGSFGST
     STVVMSDTTN NLFEAPQVYK LQGQDRYLMI VEAIGSQGRY FRSFTATSLN GSWTPQAATE
     SNPFAGKANS GATWTNDISH GELIRTNPDQ TMTVDPCNLQ LLYQGRSPAS GGDYGLLPYR
     PGLLTLQR
//
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