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Database: UniProt
Entry: G8T9H1_NIAKG
LinkDB: G8T9H1_NIAKG
Original site: G8T9H1_NIAKG 
ID   G8T9H1_NIAKG            Unreviewed;       363 AA.
AC   G8T9H1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:AEV99161.1};
DE            EC=3.2.1.37 {ECO:0000313|EMBL:AEV99161.1};
GN   OrderedLocusNames=Niako_2827 {ECO:0000313|EMBL:AEV99161.1};
OS   Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS   GR20-10).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV99161.1, ECO:0000313|Proteomes:UP000005438};
RN   [1] {ECO:0000313|EMBL:AEV99161.1, ECO:0000313|Proteomes:UP000005438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC   {ECO:0000313|Proteomes:UP000005438};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA   Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Niastella koreensis GR20-10.";
RL   Submitted (DEC-2011) 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; CP003178; AEV99161.1; -; Genomic_DNA.
DR   RefSeq; WP_014219075.1; NC_016609.1.
DR   AlphaFoldDB; G8T9H1; -.
DR   STRING; 700598.Niako_2827; -.
DR   KEGG; nko:Niako_2827; -.
DR   PATRIC; fig|700598.3.peg.2902; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_009397_4_1_10; -.
DR   OrthoDB; 3308423at2; -.
DR   Proteomes; UP000005438; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..363
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003516410"
FT   SITE            177
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   363 AA;  40852 MW;  96A51FA1ACDE1A6C CRC64;
     MKRNSFILAS AIAVICSCND AASDKAAPAS DSSTVKTTTE NNKYLSQPLV TNIYTADPSA
     HVFNGRIYIY PSHDTATGTP ENDNGDHFNM MDYHILSMDS VGGKVTDHGV ALHIKNIPWA
     GRQLWAPDAA FANNTYYLYF PVKNKQDVFQ IGVATSKTPE GPFTPEKEPI KGSYSIDPCV
     FKDDNGSYYM YFGGIWGGQL QRWNNNKYDS AGKLRQPDQQ AILPRVAKLS ADMKSFAEPV
     KEIKILDSAG NLYKEKNNDK RFFEASWMHK YHGKYYFSYS TGDTHNIVYA IGDSPYGPFT
     YKGLLLAPVE GWTNHHSIIE KDGKWYLFYH DIQLSGKTHL RNVKVTQLFY NPDGSIQTVH
     SQK
//
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