ID A0A1G5QH83_9MICC Unreviewed; 529 AA.
AC A0A1G5QH83;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:SCZ60691.1};
GN ORFNames=SAMN02799638_02985 {ECO:0000313|EMBL:SCZ60691.1};
OS Arthrobacter sp. UNCCL28.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1502752 {ECO:0000313|EMBL:SCZ60691.1, ECO:0000313|Proteomes:UP000199526};
RN [1] {ECO:0000313|EMBL:SCZ60691.1, ECO:0000313|Proteomes:UP000199526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCCL28 {ECO:0000313|EMBL:SCZ60691.1,
RC ECO:0000313|Proteomes:UP000199526};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMWE01000005; SCZ60691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5QH83; -.
DR STRING; 1502752.SAMN02799638_02985; -.
DR Proteomes; UP000199526; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09001; GH43_FsAxh1-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT DOMAIN 320..499
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 132
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 529 AA; 57917 MW; F4B230371500E924 CRC64;
MTTMGNRHRT PEYGNPILNA DWPDPDAVQV GGTYYLIASS FNRVPGLPVL RSTNLVDWEH
IGHALAELPQ TSHYSLVRHG SGVWAPALRY HDGKFWIFYP DPDHGIFVLS ADKAEGPWSA
PHLLYAGRGL IDPCPLWDDD GQAYLVHGWA KSRIGVKNRL TVHRMSPDAT RLLDHGTHVI
NGEDLPGFTT LEGPKFYKRD DWYWIFAPAG GVSTGWQSVF RSRSPFGPYQ ERRVLEQGDS
PVNGPHQGAW VTTPEGQDWF LHFQDRGAYG RVVHLQPMGW DADGWPWMGK TADDGGPGTP
VLTHPYPAGT SPEAVAPPAS DNFTSPGLGP QWHWQANPRK EWLSTCGGGH LVLRPQANDP
INLRELPNVL GQILPGVPST FTTTLELDDV PAGTRAGVVV LGQRYAWLGI VRTGDGYVLG
SGTGSEGPHE LPVGRAVDLP GPRIELQIRT DQTPRASFAW RVGPTDPWQI PLWDFDVVEG
RWIGAELGIF TASPLGSRES GSVIVGPVRV ETSPVRRSTA PRIAAAVSP
//
