UniProt: C9RK54

Database: UniProt
Entry: C9RK54_FIBSS

LinkDB:  C9RK54_FIBSS 
Original site:  C9RK54_FIBSS

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Ontology (3)   
   GO (2)   
   CAZY (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (1)   
All databases (15)   

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ID   C9RK54_FIBSS            Unreviewed;       327 AA.
AC   C9RK54;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
GN   OrderedLocusNames=FSU_2741 {ECO:0000313|EMBL:ADL25949.1};
OS   Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL25949.1, ECO:0000313|Proteomes:UP000000517};
RN   [1] {ECO:0000313|Proteomes:UP000000517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517};
RA   Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA   Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT   "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681,
CC         ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097,
CC       ECO:0000256|RuleBase:RU362015}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015}.
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DR   EMBL; CP002158; ADL25949.1; -; Genomic_DNA.
DR   RefSeq; WP_014546846.1; NC_017448.1.
DR   AlphaFoldDB; C9RK54; -.
DR   STRING; 59374.FSU_2741; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   GeneID; 34756549; -.
DR   KEGG; fsc:FSU_2741; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_753868_0_0_0; -.
DR   OrthoDB; 9806342at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000517; Chromosome.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU01097}; Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..327
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003002218"
FT   DOMAIN          36..249
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        236
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   327 AA;  36155 MW;  FAFBA8958DF6A51B CRC64;
     MRNSKFFVLS LAVAFATEAY SQDFCNTATH SGESTVVTSN DINDIGNYSY ELWADIGNNS
     ATFYTDGSFS CEFNNVNDYL CREGIRYGMN SGLKYTDLGH LYADFKLTDP KFSSYTNVTY
     SYIGVYGWSQ DPLIEWYIVD NWSPYRPNWI GKSTANCDEC GLRGTITVDG ATYEVYVDKV
     QRGSIEGDNT PFTQYFSVRK SKRSCGTIDI TAHFDGWKSL GLELGNSMYE AKVLGEAGQY
     PENGNASGTL DFAYAKVYTS EASSTALPQF APKTNTITSA QVFDMQGKFL GNVNATSDIQ
     SAIKNKFHST GIYMVKLGSA MKSVSVK
//

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