ID C6W282_DYAFD Unreviewed; 346 AA.
AC C6W282;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:ACT92055.1};
DE EC=3.2.1.37 {ECO:0000313|EMBL:ACT92055.1};
GN OrderedLocusNames=Dfer_0795 {ECO:0000313|EMBL:ACT92055.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT92055.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT92055.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP001619; ACT92055.1; -; Genomic_DNA.
DR RefSeq; WP_015810312.1; NC_013037.1.
DR AlphaFoldDB; C6W282; -.
DR STRING; 471854.Dfer_0795; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; dfe:Dfer_0795; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_1_10; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000002011; Chromosome.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 158
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 346 AA; 38602 MW; 1777AB236B2A9301 CRC64;
MISFNKLLIA FAAGTGSLYA QNDAVKIQPL VTDLYTADPS AHVFNGKIYI YPSHDVEAHV
AQDDEGGHFQ MRDYHVYSMD KIGGKVTDHG RVLDVKDVPW ADKQMWAPDA AFKNGTYYLY
FPAKDKQGIF RIGVATSKSP SGPFKAQPEP IAGSYSIDPA VFTDADGKSY MYLGGIWGGQ
LQRWHSGTYD KTLMTDLGKG HENESALSAK VALMSGDMLS FAEPLRDVQI LDTNGKPLLA
ADNDRRFFEG AWMHKYNGKY YFSYSTGDTH LLCYAEGSSP YGPFTYKGVI MNPVEGWTTH
HSIVEFDGKW YLFYHDSALS GKTHLRNVKV RELLRDEAGN IKTINP
//
