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Database: UniProt
Entry: A0A1D8PB11_9FLAO
LinkDB: A0A1D8PB11_9FLAO
Original site: A0A1D8PB11_9FLAO 
ID   A0A1D8PB11_9FLAO        Unreviewed;       962 AA.
AC   A0A1D8PB11;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=LPB138_14225 {ECO:0000313|EMBL:AOW21764.1};
OS   Urechidicola croceus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Urechidicola.
OX   NCBI_TaxID=1850246 {ECO:0000313|EMBL:AOW21764.1, ECO:0000313|Proteomes:UP000176050};
RN   [1] {ECO:0000313|EMBL:AOW21764.1, ECO:0000313|Proteomes:UP000176050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0138 {ECO:0000313|EMBL:AOW21764.1,
RC   ECO:0000313|Proteomes:UP000176050};
RA   Kim E., Yi H.;
RT   "Lutibacter sp. LPB0138, isolated from marine gastropod.";
RL   Submitted (OCT-2016) 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};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097}.
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DR   EMBL; CP017478; AOW21764.1; -; Genomic_DNA.
DR   RefSeq; WP_070237924.1; NZ_CP017478.1.
DR   AlphaFoldDB; A0A1D8PB11; -.
DR   STRING; 1850246.LPB138_14225; -.
DR   KEGG; lul:LPB138_14225; -.
DR   OrthoDB; 1447653at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000176050; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd12215; ChiC_BD; 1.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.60.40; -; 2.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR031768; CBM60_xylan-bd.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR002509; NODB_dom.
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; PF16841; CBM60; 2.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS51677; NODB; 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:UP000176050};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..962
FT                   /note="endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009110998"
FT   DOMAIN          31..218
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   DOMAIN          362..537
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          220..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..794
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   962 AA;  102909 MW;  32E55FAA80735195 CRC64;
     MKKITFFKKE VKLCLILAFL FLSFQNLTAQ TICNNEIGEQ GGYTYEYWKD QGTGCMTLEN
     GGAFSTEWND INNLLARKGL RPGSMNQTVT YTANYQPNGN SYLCVYGWTT SPLVEYYIVD
     SWGTWRPPGA TAKGTVTTDG GTYDIYETTR TQQPSIEGTQ TFQQYWSVRQ SKRTSGTISV
     ENHFNAWANL GMNMGDLYEV SLTVEGYQSS GTCEITSMSM GTSSGGGNNG GGTTNPPQDN
     GSGNITVNAR GVVGDEIINI LVNGSVAGTF TLGTSFDNYS VSGSGTVQVE YTNDDGEDRD
     VVVDYATIDG VTYQAEDQEI NTGVYQDDSC GGSYSENMHC NGYIEFGSSN TGGGNDPGSC
     NGYYALTFDD GPTSQTNELL NILNNAGVKA TFFPAGNRIN NDLASFQAMV NAGHNIENHS
     YSHSHMLDWS YQQVYDDLNQ AQQVIQSAGG GTPTLFRPPY GETNSTIISA ANDLGMNVVT
     WDVDTEDWNG ASTASIVSTA NNIQNGDVFL MHDGYSTTNN AIQQIVTNLS NSGLCAGSIN
     ENGDAVAWTQ NTTGGGGTPT CDASTITHYV SINDGSWDGM SSISVNEGDK VEIGPQPEDG
     GSWSWSGPNG YSNSSRVVTI NNATTSDAGT YTATYTNDCG TVSTSTINLS VTASNNGGGG
     TTTGNITVRA RGVVGDESID IVVGGTVAGT FTLTTSYADY SVTGSGTVQV DFTNDEGDRD
     VQVDYAIIDG TTYQAEDQEI NTAVYQDGSC GGSYSENMHC GGYIEFATNG GGTTPDPDPI
     PDPDPTPDPD PTPAGCNGLP TWTSTGVYSE TGTQVVYNGN IYENRWYSSG QNPETNSGQW
     QVWILVGSCN TGRGVNSNDT KSNDTKSNDT NIEMTVNDKN LINTPFNFVI YPTVSKNGRF
     QIQSSDEILS VQLFDINGRL IKSNFNGAKN YSVLEVNAKS GVYIAKFTTS HGEIHMKRLL
     IK
//
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