ID A0A1U9N8W5_9GAMM Unreviewed; 675 AA.
AC A0A1U9N8W5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:AQT60072.1};
GN ORFNames=B0D95_08180 {ECO:0000313|EMBL:AQT60072.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT60072.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT60072.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT60072.1,
RC ECO:0000313|Proteomes:UP000189646};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; CP019799; AQT60072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9N8W5; -.
DR STRING; 1945512.B0D95_08180; -.
DR KEGG; ceb:B0D95_08180; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000189646; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09001; GH43_FsAxh1-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
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; PF00553; CBM_2; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000189646};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..675
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012052732"
FT DOMAIN 24..133
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 135..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 305
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 675 AA; 73770 MW; 516C20C16EAC6367 CRC64;
MRANNKVSAR YAVSRIKIGG SFFALLFAWN VHASCQYQVT NQWNNGFTAA IKITNTGTGA
INNWSVNWQY SGDNRITNSW NANLSGANPY SASNLSWNAT IQPNQTVEFG FQGTKGTAAA
EVPVINGAPC GGSVTSSSRA ASSSSNATTT SSSRPASSVA MSSSSRISSN AASSSSAFNL
VEASNPTIWA DVPDPSVIRV GNTYYMSSTT MHMSPGVPIM KSTDLVNWSL INYAYSTLDN
TSALNLENGQ NAYGKGSWAS SIRYVDGTYY VSTFSYTTNK TYIYKTRDIE NGPWTVSALN
GLYHDSSLFF ENGRAFLAYG IDDIKIIELT ADASAIKPGG LNQTIITKSS SVAGTNFIVR
PEGTHLQKIN GRYYISLITW PSGKSRTQLI FRSNNLTGPY EGRIALQDQG VAQGGLVDTP
TGNWYAFLFR DSGAVGRIPY LVPVSWQDGW PVMGVSGKVP QKLGFVVEDK NLRGIVTADE
FNQGSQGSSS LPLQWQWNHN PDNSGWSLLN RPGYLRLTTK RTAANFEVAR NSLTQRTFGP
QSSARIAMET AGMKDGDYAG LGALQTRYGF VGVNKTGGNK SIVMVDTTSG SPQEITRIGL
NQDRVYFRID MDFRNQTDQG RFYYSLDGNN WTVIGSTLRM TYDLKHFMGY RFALFNYATQ
STGGYVDFDY YRLGQ
//
