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Database: UniProt
Entry: A0A1G7BG05_9ACTN
LinkDB: A0A1G7BG05_9ACTN
Original site: A0A1G7BG05_9ACTN 
ID   A0A1G7BG05_9ACTN        Unreviewed;       484 AA.
AC   A0A1G7BG05;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Beta-xylosidase, GH43 family {ECO:0000313|EMBL:SDE25902.1};
GN   ORFNames=SAMN05216270_116137 {ECO:0000313|EMBL:SDE25902.1};
OS   Glycomyces harbinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=58114 {ECO:0000313|EMBL:SDE25902.1, ECO:0000313|Proteomes:UP000198949};
RN   [1] {ECO:0000313|EMBL:SDE25902.1, ECO:0000313|Proteomes:UP000198949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDE25902.1,
RC   ECO:0000313|Proteomes:UP000198949};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; FNAD01000016; SDE25902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7BG05; -.
DR   STRING; 58114.SAMN05216270_116137; -.
DR   OrthoDB; 177947at2; -.
DR   Proteomes; UP000198949; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   CDD; cd18817; GH43f_LbAraf43-like; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF110221; AbfB domain; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..484
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011677987"
FT   DOMAIN          354..482
FT                   /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05270"
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            166
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   484 AA;  52881 MW;  45C4747ECB0DD4A2 CRC64;
     MHRAPLNRRR LFQTAGAAAL VTAASTFGIP APASAAPGVL YSNALVQQRA DPHIVRHTDG
     HYYFTASVPA YDRIIMRRST TLQGLATAQE STIWSKHSSG PMSHHIWAPE IHYIDGKWYV
     YFAAGRADDI WAIRMYVLEN AGANPMSGTW TERGQIALQR DSFSLDATTF TNGSTRYLCW
     AQSDPELGSG TSLYLAAMSN PWTITGTPVR ISKPTNSWEV IGHKVNEGAA VVKRNGRIFM
     TFSASATDAN YAVGLLTASQ SANLLSASSW TKSAQPVLRS NDNTSQFGPG HNSFTVSEDG
     QSDILVYHAR PYKAISGDPL YDPNRHTRIQ KFYWNADGTP NFGVPVADGA TPYRFAAYGA
     SGVYLNHWEF RLRANATAAM LADSQFRIVT GLAGSGTVSL ESANYPGYYL RHKNYEIWVE
     RSDGTALFRS DASFHRRSGL ADSGAVSFEA SNAAGRYLRH VDGLAYVQTA ATDAERAAAT
     FRLE
//
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