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Database: UniProt
Entry: R6RHR4_9FIRM
LinkDB: R6RHR4_9FIRM
Original site: R6RHR4_9FIRM 
ID   R6RHR4_9FIRM            Unreviewed;       602 AA.
AC   R6RHR4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:CDC47335.1};
GN   ORFNames=BN788_02219 {ECO:0000313|EMBL:CDC47335.1};
OS   [Eubacterium] siraeum CAG:80.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillospiraceae incertae sedis.
OX   NCBI_TaxID=1263080 {ECO:0000313|EMBL:CDC47335.1, ECO:0000313|Proteomes:UP000018142};
RN   [1] {ECO:0000313|EMBL:CDC47335.1, ECO:0000313|Proteomes:UP000018142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:80 {ECO:0000313|Proteomes:UP000018142};
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}.
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:CDC47335.1}.
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DR   EMBL; CBFJ010000142; CDC47335.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6RHR4; -.
DR   Proteomes; UP000018142; 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; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018142};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..602
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038528523"
FT   DOMAIN          404..597
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   REGION          28..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        256
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            203
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   602 AA;  68029 MW;  82E9DE501B174281 CRC64;
     MKRLVRFAAA LMAVLTLTAC TAEVGTSSVT STPMSTTTST STSNPLPSVT TEPGKEEDPK
     VLDKDIIKST ITSTDDGKGN YTNPVIFADV PDIDIIRVDD AFYMVSTTMH LSPGCPVMKS
     YDLVNWEIVN YVFDTLEDSD KLALRNGENN YGKGQWATTL RYNNGVYYAG FTSFSTGKTY
     IYHTDDIENG KWDRFVYDEC FHDMSLLFDD DGKVYLIYGG GEIYCVELEK DLSAVKPGTK
     RKLINNAGLV KGCLAEGSHV YKLNGYYYIF IITWPPNSKR TQLCYRSEAL DGEWERKVII
     RDNMGFRNDG VAQGGIVDDK DGNWYCFVFQ DHGAVGRTPV VSTMTWEDGW PVVGVKGKVP
     TTAKIPIAGH EKKGIVTSDE FINSHIVRSY HSFADTPEEA GESDYNGSNL GLEWQWNHNP
     DNRLWSLTER EGYLRLRTVD VCGTVANARN TISQRTFGPE CGAYIKLDVS EMKEGDVAGF
     AAFAEKYGYV AVKIEDGKKY IVTVWYDDND DVEKEFETER VEITENEVYL RVDCDFKNAT
     DKAYFYYSLD GENWTKIGDT LQMNYYGLHF MGYRYAIFNF PTKQTGGYVD VDYFRVENKL
     LK
//
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