ID A0A212TGP3_9BACT Unreviewed; 536 AA.
AC A0A212TGP3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:SNC65050.1};
GN ORFNames=SAMN06265337_1205 {ECO:0000313|EMBL:SNC65050.1};
OS Hymenobacter gelipurpurascens.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=89968 {ECO:0000313|EMBL:SNC65050.1, ECO:0000313|Proteomes:UP000198131};
RN [1] {ECO:0000313|EMBL:SNC65050.1, ECO:0000313|Proteomes:UP000198131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11116 {ECO:0000313|EMBL:SNC65050.1,
RC ECO:0000313|Proteomes:UP000198131};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FYEW01000001; SNC65050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212TGP3; -.
DR Proteomes; UP000198131; 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}.
FT DOMAIN 354..530
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 57
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 168
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 536 AA; 58548 MW; B04409ADC06ACB54 CRC64;
MSFTVESAAH FAADLSLPPK GCASNEATQT AVHLAPPVAS EPVTSYANIV LPGDFPDPTI
AQIGDTYWAS ATSAEWGPVF PLFKSSNLVD WELVSHVFPT TDTIPEWAGT NFWAPEIFHE
NGKTYVYYTA RQKGRNGRLS IGVASADDPA GPYTDHGPLV GQRQGSIDGF PMRDEHGKLY
LVWKEDGNAY QNPTPIWAQR INDTHTALVG KKVELFRNDP STWEGCLVEG SAIIRHDDYF
YMFYAGNGCC GKCCTYATGV ARAKSLLGPW EKCPQNPILK KNATWKCPGH GTVAQYQGRW
FLLHHAYYNQ SHEFVGRQGI LSEFTFNAEG WPEFEGNSPQ AAPLKDVRVL NITENFAGNC
LAGTWQWPIG QQPEVGVADG QLLLTANPRG IGSVVAQRTF TATYKATTSL ATSSLDHDTF
AGLCAIGDPD NALALVAGNG TLQVWHVKGG HHQSLAKLTL PAGPTLHLRL EAWGGQRFRF
TYGTDGSTWQ PVLLDSFALN GEYLPPWDRG VRVGLLAQGL DSATVAFNDF AIRNQR
//