UniProt: C9RLL3

Database: UniProt
Entry: C9RLL3_FIBSS

LinkDB:  C9RLL3_FIBSS 
Original site:  C9RLL3_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 (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
All databases (14)   

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ID   C9RLL3_FIBSS            Unreviewed;       367 AA.
AC   C9RLL3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 83.
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_3006 {ECO:0000313|EMBL:ADL25314.1};
OS   Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL25314.1, 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; ADL25314.1; -; Genomic_DNA.
DR   RefSeq; WP_014547057.1; NC_017448.1.
DR   AlphaFoldDB; C9RLL3; -.
DR   SMR; C9RLL3; -.
DR   STRING; 59374.FSU_3006; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   GeneID; 34756790; -.
DR   KEGG; fsc:FSU_3006; -.
DR   PATRIC; fig|59374.8.peg.2876; -.
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   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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..367
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003002253"
FT   DOMAIN          34..244
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   REGION          273..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        231
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   367 AA;  39627 MW;  735E0D2A8545E2E0 CRC64;
     MVNKIIIALS MGLTAGVLAQ DFCNAAKHTG ASKKVNGNEV SSFNGVGYEL WYDRATSGSL
     TIYEDGSMAC SFQNAGDYLC RAGLSFDSDK KYNELGGDML AEFKLVKQNI NGADYSYVGV
     YGWMEEVSKS PSKLVEYYVV DNWLTGWRPG DWVASHKMGD YTIDGAKYSV YWGEHTGPAI
     KTQGNTTFLQ YFSIRENARD CGVINISAHM RQWEKLGMEM GKLYEAKVLG EAGSMSNGVS
     GTADFPHIKV YVKGDEVPSS SSVALSSSSV VSSSSETVPS SSSEKVAESS SSVDGSSSSG
     TDAIPFMAQL FDKAGVYQVF DMQGNFLGKV ELKNGLSLKQ AVASKFARSS VYLVKRGAFA
     KTIAVER
//

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