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
//