ID   F4QN79_9CAUL            Unreviewed;      1001 AA.
AC   F4QN79;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative beta-xylosidase {ECO:0000313|EMBL:EGF91670.1};
GN   ORFNames=ABI_30870 {ECO:0000313|EMBL:EGF91670.1};
OS   Asticcacaulis biprosthecium C19.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF91670.1, ECO:0000313|Proteomes:UP000006512};
RN   [1] {ECO:0000313|Proteomes:UP000006512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA   Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Draft genome sequence of Brevundimonas diminuta.";
RL   Submitted (MAR-2011) 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; GL883078; EGF91670.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4QN79; -.
DR   STRING; 715226.ABI_30870; -.
DR   eggNOG; COG1621; Bacteria.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_299506_0_0_5; -.
DR   Proteomes; UP000006512; 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; cd08984; GH43-like; 1.
DR   CDD; cd09001; GH43_FsAxh1-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR008999; Actin-crosslinking.
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; SSF50405; Actin-crosslinking proteins; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1001
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003314266"
FT   DOMAIN          363..547
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        55
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            164
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   1001 AA;  110645 MW;  5B4522253574ECD7 CRC64;
     MRSFIAGLVI VVGLGLAGIT TAYAQETPTT WPTTWTADNG NGTFTNPLFY DEFSDPDMIR
     VGDDYYLTGT TMHSMPGLPL LHSKDLVNWT FLTYVSPKLD LGPGFRLEDG KGVYGQGIWA
     PTFRYHDGKY YIFSNVNGQT TQLFTATDPK GPWTHAQMKR SFHDLSVLFD GGKAYIIWGY
     QGIRMAELNA ELSDIVPGTE REIIPHSAGM GEGVHFYKLN GKYYITSAWF DGRMRMPAAR
     ADTIWGPYDV NQAISIDEDF GLAEGNRVGG RQPFLRIHPG NPAPNGRMSL HQGGLVQTPE
     GEWWGFSMMD YNSVGRLTAL APITWKDGWP YFGLPGNLTR NPRTWVKPKT KYKVAPHMPY
     ERSDDFAGAT LKPVWQWSHV PVDAKWSLTE RPGHLRLHTL SAADFWTARN TLTQRAIGPQ
     STPTAVLDAA GLKPGDVAGL ALTNKPYAWI GVERGDDGLF LVQFNEYTNA TTRVKIDATK
     VWLRAEADFM TEIARFSYST DGETWLPTGE PFTMAFQLIT FQGVRYSLFA YNTRRAEGGY
     ADFDSIDVYE PHPRGLMKPI PYGQSIRLTS WAAPTGLGVT DGKPNRGAPA DVAVVDMKLG
     RAALKFGDAF LTVAADGAVS LKTGKPGTAQ SFQWIETPTG ELALMSLVTN RFLRIDPQTG
     AVVADSPGPQ SDGKDGVRFT WAPALKVAQK PLYRDPVYDG AADVSIVWDD AQARWTMFYT
     NRRATVKAPD LKDVAWVHAT PIGVATSADG LSWDYSGTAV FPAQCTGTTL WAPEVFRGED
     RDGEGYHMWL TIVPGIFNRW GQPGATSRIV HLTSPDLKTW SCAGDVELDI GRIIDAAVIK
     VGDTYRLWYK DETVGSRIMA ADSADMKTWK RVGDTPVSET RGEGPKVFRL AGKYWMVFDA
     WKGLAVLSSD DATTWVQQDG FILAEPGMNP TDRAKGQHPD VVVSGDRAFI YYFVHQGAEK
     PEDPHWNQRT VIQVAELKLV DGKLTVDRNA DVDALLAPPV R
//