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
//