ID A0A0S8F9A6_9BACT Unreviewed; 380 AA.
AC A0A0S8F9A6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:KPK57312.1};
DE Flags: Fragment;
GN ORFNames=AMK73_10290 {ECO:0000313|EMBL:KPK57312.1};
OS Planctomycetes bacterium SM23_32.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704029 {ECO:0000313|EMBL:KPK57312.1, ECO:0000313|Proteomes:UP000052164};
RN [1] {ECO:0000313|EMBL:KPK57312.1, ECO:0000313|Proteomes:UP000052164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_32 {ECO:0000313|EMBL:KPK57312.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK57312.1}.
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DR EMBL; LJUE01000236; KPK57312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8F9A6; -.
DR PATRIC; fig|1704029.3.peg.447; -.
DR Proteomes; UP000052164; 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}.
FT DOMAIN 304..380
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 120
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"
FT NON_TER 380
FT /evidence="ECO:0000313|EMBL:KPK57312.1"
SQ SEQUENCE 380 AA; 42668 MW; 836330CD01F05975 CRC64;
MRYTNPVIPG FYPDPSVCRV GRDYYLATST FEYFPGVPVF HSRDLVHWRQ IGHCLTRPEQ
LPLEGVASSE GIFAPSLRHH DGRFYMVTTN VNGGGHFYVH ADDPAGPWSD PVWVKGGGFD
PDLFFAPDGT VYFIHQEWGH GIRQWEIDVG SGRLSGEGRS IWRGLEDQFC EAPHIYHVEG
RYYLIVAEGG THRGHMVVCG RSDGPEGPFE SCPHNPILTH RARVELPIQA TGHGDLVQAH
DGSWWILFLG IRPVWGAHHL GRETFLAPVT WENGWPAVNG GEPVSLEMKA DGPPAHPWPA
EPVRDDFEAP ELRLGWNFRR NPHAEDWSLA ERPGWLALHG SELTLDDAGS PAFLGRRQRH
FDCRAACLIE FEPTRDGEEA
//
