GenomeNet

Database: UniProt
Entry: R6YQ16_9BACT
LinkDB: R6YQ16_9BACT
Original site: R6YQ16_9BACT 
ID   R6YQ16_9BACT            Unreviewed;       556 AA.
AC   R6YQ16;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Xylosidase/arabinosidase {ECO:0000313|EMBL:CDD20452.1};
GN   ORFNames=BN769_00530 {ECO:0000313|EMBL:CDD20452.1};
OS   Prevotella sp. CAG:732.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262934 {ECO:0000313|EMBL:CDD20452.1, ECO:0000313|Proteomes:UP000018039};
RN   [1] {ECO:0000313|EMBL:CDD20452.1, ECO:0000313|Proteomes:UP000018039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:732 {ECO:0000313|Proteomes:UP000018039};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDD20452.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBGP010000135; CDD20452.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6YQ16; -.
DR   Proteomes; UP000018039; 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; cd18617; GH43_XynB-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:SF12; BETA-XYLOSIDASE-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:UP000018039};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..556
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004437955"
FT   DOMAIN          386..555
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        230
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            165
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   556 AA;  61937 MW;  2100DB3E66DF8C9D CRC64;
     MKKLAILPLS CMLALGAHAQ TAEFDYFKYA GNDARFNVEI DKSHQYYNPV LAGFYPDPSL
     CRVGDTYYLV NSSFTFFPGV PLSTSKDLVN WQPAGHVLDR PSQVPLKGQN VSGGIFAPAI
     SYNKKNKTFY MITTNVGAGN FFVKSKDPSK GWSEPIYLPK IDGIDPSFFF DDNGKGYIVH
     NGPVVGGADY EGQRAIRLFE FDVKGDSIKG DFKQILRGGT HVEAKPIWIE GPHLFKKDKY
     YYLMCAEGGT GGWHSEVILR AKNPTGPWEE CPNNPILTQR TGLDPNRKDP VSSAGHADIV
     EDGKGNWWAV FLACRPYEED MYNTGRDTYL LPVTWKNGWP EILAKNTPIA TVGEKAGLKP
     AEKNEFSGNF SYTDNFEACD GKNGLKQLNS RWMFLRDFTD CYKVENGKLT LNLLPGNIYK
     REPMSAIWAR QQHGTFTAET SLNFTPRNDK DIAGLALLQK EDHNFVLGKT MKNGKLMLTL
     TRAEKNNVTI ASTPIKDGEL RLKVEGHGRY YDFFYAEQGG DWQLLAKGVD ASNLSTQKSG
     GFIGAVIGLY ASSNKE
//
DBGET integrated database retrieval system