ID A0A069D1U7_9BACE Unreviewed; 558 AA.
AC A0A069D1U7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:GAK36402.1};
GN ORFNames=JCM15093_1562 {ECO:0000313|EMBL:GAK36402.1};
OS Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK36402.1, ECO:0000313|Proteomes:UP000027601};
RN [1] {ECO:0000313|EMBL:GAK36402.1, ECO:0000313|Proteomes:UP000027601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK36402.1,
RC ECO:0000313|Proteomes:UP000027601};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(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:GAK36402.1}.
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DR EMBL; BAJS01000006; GAK36402.1; -; Genomic_DNA.
DR RefSeq; WP_024996333.1; NZ_BAJS01000006.1.
DR AlphaFoldDB; A0A069D1U7; -.
DR STRING; 1121097.GCA_000428125_00707; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000027601; 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:UniProtKB-KW.
DR CDD; cd09001; GH43_FsAxh1-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:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-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:UP000027601};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..558
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001659818"
FT DOMAIN 344..555
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 158
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 558 AA; 62369 MW; 4ECE796E09EC5934 CRC64;
MKKLALIIGL SLFVTSSVTA QKNYVSEVWV ADKGDGTYRN PIIHADYSDP DACRVGDDYY
MTSSSFNCLP ALQILHSKDL VNWTIIGAAV PYKLSPVEFP EKPQHGSRVW APSIRYHKGE
FYIFWGDPDQ GAFMTKAKDP KGPWSEPVLV KAGKGIIDTT PLWDEDGKVY MVHGYAGSRS
GIKSLLGICE LNADATKAIT QSRIIFDGHD EHPTAEGPKF YKRNGYYYIF APAGGVATGW
QLVLRSKNVY GPYEEKVVLS QGKTNVNGPH QGAWVDTTTG EDWFLHFQDV GAYGRLVHLQ
PMKWVNDWPV IGVDKDGDGC GEPVLSYKKP NVGKNYPICT PQESDEFDGY TLSPQWQWHA
NINEKWAYFA GHKGYARLYS YPVVKEYKNL WNVPNLMLQK APADNFVATI KLDFKPTTKY
KGERTGLVVM GFSYAGLVLE NTNDGIVLSQ LECKNADKGT AEQINETTKL KNGAIYLRVE
FKAGKKKLKE SEGGSDVLAM CKFSYSLDGK KFKSMGNEFQ AKEGMWIGTK VGTFCTRPAI
TINDGGWSEV DWFRITKK
//
