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Database: UniProt
Entry: A0A1U9NEX5_9GAMM
LinkDB: A0A1U9NEX5_9GAMM
Original site: A0A1U9NEX5_9GAMM 
ID   A0A1U9NEX5_9GAMM        Unreviewed;       354 AA.
AC   A0A1U9NEX5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=B0D95_19285 {ECO:0000313|EMBL:AQT62014.1};
OS   Cellvibrio sp. PSBB023.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT62014.1, ECO:0000313|Proteomes:UP000189646};
RN   [1] {ECO:0000313|EMBL:AQT62014.1, ECO:0000313|Proteomes:UP000189646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSBB023 {ECO:0000313|EMBL:AQT62014.1,
RC   ECO:0000313|Proteomes:UP000189646};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; CP019799; AQT62014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9NEX5; -.
DR   STRING; 1945512.B0D95_19285; -.
DR   KEGG; ceb:B0D95_19285; -.
DR   OrthoDB; 9763050at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000189646; 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   Gene3D; 2.60.60.40; -; 1.
DR   InterPro; IPR031768; CBM60_xylan-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
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; PF16841; CBM60; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189646};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..354
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012414394"
FT   DOMAIN          29..226
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   REGION          221..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   354 AA;  37861 MW;  9FD762FBA595D584 CRC64;
     MKLHIKGKNI FTAFIGAAAL CATVANAQTL SSNSTGTHNG FYYSFWKDSG NATMTLQAGG
     RYTSQWNSGT NNWVGGKGWN PGNSTRVINY SGSYNVSNSQ NSYLALYGWT RSPLIEYYVI
     ESYGSYNPAS CSGGTDYGSF QSDGATYNVR RCQRVNQPSI DGNQTFYQYF SVRNPKKGFG
     NISGTITFAN HVNFWASKGL NLGNHNYQVL ATEGYQSTGS SDITVSEGTS GGGGSSSSAP
     SGGNKTIVVR ARGTTGQEQI RLKVNNTTVQ TWTLSTTMSN YTATTNLSGG SLVEYFNDSG
     NRDVQVDYIS VNGSIRQSEA QTYNTGVYQN GSCGGGNGGS EWMHCNGAIG YGNL
//
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