ID L0FYL8_ECHVK Unreviewed; 374 AA.
AC L0FYL8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:AGA78133.1};
GN OrderedLocusNames=Echvi_1878 {ECO:0000313|EMBL:AGA78133.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA78133.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-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}.
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DR EMBL; CP003346; AGA78133.1; -; Genomic_DNA.
DR RefSeq; WP_015265694.1; NC_019904.1.
DR AlphaFoldDB; L0FYL8; -.
DR STRING; 926556.Echvi_1878; -.
DR KEGG; evi:Echvi_1878; -.
DR PATRIC; fig|926556.3.peg.1995; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_1_10; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000010796; Chromosome.
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; 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:UP000010796};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..374
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003942911"
FT SITE 180
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 374 AA; 42014 MW; 445D8570973EEAED CRC64;
MKKSLKRFLF TFAMGATMLS FSQCGSKTST ESTTEADSFT HKDTISYLSQ PLITDHFTAD
PSAHVFEDKI YIYPSHDIPS SAQEDDTGAQ YDMKDYHVYS MDSPNGKVTD HGEVLHVADV
AWATKQMWAP DAAEKNGKYY LYFPAKDKEN IFRLGVAVSD DPAGPFEPQP APMNGSFSID
PAVFEDRDGT HYIYWGGIWG GQLQKWRTGK YHSTGDSPFA DEPADEEPAI APKVAKLSGD
MLEFGEKPKD ILILDQAGEP IKAGDHDRRF FEAAWVHRHD DTYYFSYSTG DTHTISYATG
DNPYGPFTYQ GVVLAPVQGW TNHHSIVKVG DQWYIFYHDT QISGKNYLRN IKMAPLQHNP
DGSIQTIIPM EKTK
//
