ID K6U662_9CLOT Unreviewed; 512 AA.
AC K6U662;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:EKQ50484.1};
GN ORFNames=A370_05488 {ECO:0000313|EMBL:EKQ50484.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ50484.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ50484.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:EKQ50484.1}.
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DR EMBL; ALXI01000173; EKQ50484.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U662; -.
DR STRING; 1196322.A370_05488; -.
DR PATRIC; fig|1196322.3.peg.5352; -.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000001325; 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; cd18617; GH43_XynB-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:SF12; BETA-XYLOSIDASE-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001325}.
FT DOMAIN 319..512
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 122
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 512 AA; 58331 MW; 4DCB5C3A9831B482 CRC64;
MNKIKNPILS GFYPDPSICA VGEDFYLVTS TFAYFPGVPI FHSKDLVNWR QIGNVLTRKS
QLNLEGAGHS QGIFAPTLRY NNGIYYLITT NISHGGNFIV TAEKPEGPWS DPYWLEGAIG
IDPSLFFDDD GKAYYIGTRP NPEGVRYNGD WEVWIQELDL NNMCLVGDSH KIWKGALRDV
IWPEGPHLYK KDDYYYLMIA EGGTGPEHCV TIARSAFIYG KYEGCPRNPI ITHRHLGKSY
PIKHVGHGDL VKTQDDKWFM VMLASRTCDG YCNTGRETFL AKVTWEGGWP VANPGSGILE
LEQDHELLEY EVEPKESCYH FYGKELDNTW VFLRNPSENL YSLTEKEGCL RLYLKEQSLK
DLDNPAYIGI RQKEYHYIIS TMMEFNPNNE NESAGIAIVQ SNEYHIRYEC TQRNGREVLQ
IIECNNGKDI LINEVEINSS KLCLKMVSKG QKLDLYYGID GTSYKLLQKD VSTKNLSTEV
AGGFVGCTIG MYASSNGKTT DNYADFYWFE YK
//
