ID A0A081PDL6_9SPHI Unreviewed; 504 AA.
AC A0A081PDL6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KEQ28789.1};
GN ORFNames=N180_19240 {ECO:0000313|EMBL:KEQ28789.1};
OS Pedobacter antarcticus 4BY.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ28789.1, ECO:0000313|Proteomes:UP000028007};
RN [1] {ECO:0000313|EMBL:KEQ28789.1, ECO:0000313|Proteomes:UP000028007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4BY {ECO:0000313|EMBL:KEQ28789.1,
RC ECO:0000313|Proteomes:UP000028007};
RA Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA Reddy G., Bhargava P.M.;
RT "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT Soils of Schirmacher Oasis, Antarctica.";
RL Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ28789.1}.
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DR EMBL; JNFF01000106; KEQ28789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081PDL6; -.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000028007; 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; cd08999; GH43_ABN-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:SF5; ENDO-ARABINASE; 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:UP000028007};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..504
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001761649"
FT DOMAIN 320..460
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 143
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 504 AA; 56420 MW; 689FF3AE5AE013FD CRC64;
MRQRLLLLAA VHLILLSNVV SAQNAIHPVI PGDFADPSII RADNKYYAIG TSSEWAPHFP
IYTSSDLINW KQTGYLFDKA PAWTMGSFWA PEYDYHDGTY YIYYTARRKK DQISCIGVAT
SKYPDKGFVD HGVIIDHGKE AIDAFVFLDK GTRYMTYKAY GLDDRPIEIL GVKLSKDGLR
SEGEPFSMLK DDQRKGLEGQ SILKKDNYYY LFYSAGNCCG IQCDYNVGVA RSKSFEGPYE
KYAGNPLLAE NASWKCSGHG TFAEGANGKL YYLYHAYNKQ TALFSGRQGM LAELIWPGQN
EWPLLKEQSG PELNPDIKLS FKNSSLDLGW QWDFRNSGTL VSQNAENLHL SGKVNDDNLA
GIALTRRPVS GVFEALTTVV NSNNALKGLT YYGDATAAVG VGVTGNTVQF WSVQNKANKI
LASAHLPTNE QVQLKLKTTA DLRITAFFKQ GNQEWQELKV TEEPKAESLT QWDRSPRIGL
HFKGKPAEEA VFSSFDLKYM PQQN
//
