ID A0A345SRY2_9ACTN Unreviewed; 482 AA.
AC A0A345SRY2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C7M71_002380 {ECO:0000313|EMBL:AXI76487.1};
OS Peterkaempfera bronchialis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Peterkaempfera.
OX NCBI_TaxID=2126346 {ECO:0000313|EMBL:AXI76487.1, ECO:0000313|Proteomes:UP000249340};
RN [1] {ECO:0000313|Proteomes:UP000249340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 106435 {ECO:0000313|Proteomes:UP000249340};
RA Batra D., Gulvik C.A.;
RT "Streptacidiphilus bronchialis DSM 106435 chromosome.";
RL Submitted (JUL-2018) 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}.
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DR EMBL; CP031264; AXI76487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345SRY2; -.
DR KEGG; stri:C7M71_002380; -.
DR OrthoDB; 3317993at2; -.
DR Proteomes; UP000249340; Chromosome.
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:UP000249340};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..482
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016955380"
FT DOMAIN 29..153
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 156..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 50447 MW; 716E69E4389989E8 CRC64;
MVAGTAVGTA IAFVGMTTAA THAVAGTGTG TVKGVGSGRC LDVPNSSTAD GTLVQLYDCN
SNSNQQWTYT ADNELKVLGS KCLDAAGSAS GAKVQTYGCW GGDNQKWRIN ADGSIVGVQS
GLCLDAISAG TANGTKLQLY SCTSGSNQKW TFSGDASTTT GGTTAGTTTG TTGGGTGGTG
GTCSLPSTYR WTSTGVLAEP KNGWVALKDF TNVMYNGKHL VYASNVSGST YGSMAFTPFT
NWSDMASTGQ TGMSQATVAP TLFYFAPKNI WVLAYQWGSW PFIYRTSSDP TNPNGWSSPQ
PLFTGSISGS STGPIDQTLI ADGQNMYLFF AGDNGKIYRA SMPIGNFPGS FGSSYTTVMS
DSQNNLFEAV QVYKVQGQNQ YLMIVEAIGA NGRYFRSYTA SSLSGSWTPQ ATSESSPFAG
KANSGATWTN DISHGDLVRD NPDQTMTIDP CNLQLLYQGK SPTAGGSYDQ LPWRPGVLTL
QH
//
