ID A0A0Q6WF99_9BURK Unreviewed; 509 AA.
AC A0A0Q6WF99;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0000259|Pfam:PF17851};
GN ORFNames=ASD15_30310 {ECO:0000313|EMBL:KQV85927.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV85927.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV85927.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV85927.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV85927.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV85927.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KQV85927.1}.
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DR EMBL; LMDJ01000009; KQV85927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6WF99; -.
DR Proteomes; UP000051876; 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; cd09002; GH43_XYL-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:SF2; XYLOSIDASE_ARABINOSIDASE; 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:UP000051876}.
FT DOMAIN 327..497
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 138
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 509 AA; 56836 MW; FF3F1CAC39754815 CRC64;
MGNPFLRHCQ DWARGIEQQR KADLGNGTYL NPIMAGDHPD PSVLKDGDDY YMTFSSFEAY
PGLTIWHSRD LVNWEPIGSA LKKYIGSVWA PELAKHKGRY YLYIPAKLPG NNNIYVVHAD
NIRGPWSEPV ALGNTRIDPG HIVGEDGKRY LFLSHGDRVQ LSDDGLKIVG PMQHVYDGWK
YPEHWDVEGY AQEGPKMTRH GDYYYMTLAL GGTAGPPTGH MVVSARSKSI HGPWENSPYN
PIIRTESAAE KWWSKGHATL VEGPGKSGWY MMYHGYENGF HALGRQALLA PIVWTEDGWF
KASEHDAGKP IPKPAGGSAV PHGMALSDDF STNKFGLQWS FFRGGIDENQ RVRYRDGVLE
LEAKGSSPAN SSPLTFLAGD QAYQFEVDID FDEGAQAGAL LFYNDKLYAG VGVNKGAFIL
HRYGMDQPRG EKPAGMANKL RMRVTNDRHI MTIHTSIDQG KTWHKYGVQM EVSGYNHNVA
YGFMSLRPAI YASGKGKVRF SNLVYRALP
//
