GenomeNet

Database: UniProt
Entry: Q3BZD2_XANC5
LinkDB: Q3BZD2_XANC5
Original site: Q3BZD2_XANC5 
ID   Q3BZD2_XANC5            Unreviewed;       527 AA.
AC   Q3BZD2;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Xylosidase {ECO:0000313|EMBL:CAJ21781.1};
DE            EC=3.2.1.37 {ECO:0000313|EMBL:CAJ21781.1};
GN   Name=xylB1 {ECO:0000313|EMBL:CAJ21781.1};
GN   OrderedLocusNames=XCV0150 {ECO:0000313|EMBL:CAJ21781.1};
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN   [1] {ECO:0000313|EMBL:CAJ21781.1, ECO:0000313|Proteomes:UP000007069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10 {ECO:0000313|EMBL:CAJ21781.1,
RC   ECO:0000313|Proteomes:UP000007069};
RX   PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneicker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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; AM039952; CAJ21781.1; -; Genomic_DNA.
DR   RefSeq; WP_011345889.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BZD2; -.
DR   STRING; 456327.BJD11_22185; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   KEGG; xcv:XCV0150; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_039823_0_0_6; -.
DR   Proteomes; UP000007069; Chromosome.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd09002; GH43_XYL-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:SF2; XYLOSIDASE_ARABINOSIDASE; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..527
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004224839"
FT   DOMAIN          346..523
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        58
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            159
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   527 AA;  58263 MW;  D2C78E2B0F0FB484 CRC64;
     MRVRPISSRW RWPMAGGLLL CAGLSAAADW KRGIEHQRIA DQGDGSFLNP VLAGDHPDPS
     VLKDGDDYYL TLSSFDAYPG LPIWHSRDLV NWQPLGHAIT QNVGAIWAPD LIKHGKRYYI
     YFPARRGDQG ERSNFVVWAD DIKGPWSAPI DIGLGKYIDP GHAVGEDGKR YLFLSGGDYV
     QLSDDGLKVV GTPKHVYDGW KYPESWDVEG YAQEGPKITR HNGWYYMTTA VGGTAGPPTG
     HMVITARSRS IHGPWQNAPN NPITRTRSAQ EPWWSRGHAT LVEGTDKRWW MLYHGYENGY
     WTLGRQALLD PIEWTPDGWF VAKGGDLGTP LKKPSGQALP HGLALSDDFR ASTLGPQWAF
     FNPAADEAKR LQVGNGVLRL QGKGSAPRDA SPLTVIATDP AYQFEVQMTV SPGGQGGALL
     FYSDKLYAGV GSNGQQFVMH RYGEERPATL APSTNGGTLW LRVTNNRHIV TIHSSTDGKA
     WTKYPVQMEV SGYHHNVAGK FLALKPALYA AGPGQVEFRN FRYRALD
//
DBGET integrated database retrieval system