ID C5BU23_TERTT Unreviewed; 685 AA.
AC C5BU23;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=TERTU_1680 {ECO:0000313|EMBL:ACR11346.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR11346.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR11346.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR11346.1; -; Genomic_DNA.
DR RefSeq; WP_015817458.1; NC_012997.1.
DR AlphaFoldDB; C5BU23; -.
DR STRING; 377629.TERTU_1680; -.
DR CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR CAZy; CBM60; Carbohydrate-Binding Module Family 60.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR KEGG; ttu:TERTU_1680; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_417813_0_0_6; -.
DR OrthoDB; 9763050at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000009080; Chromosome.
DR GO; GO:0030248; F:cellulose 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 Gene3D; 2.60.120.180; -; 1.
DR Gene3D; 2.60.60.40; -; 1.
DR Gene3D; 2.30.32.30; CBM10; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR036601; CBM10_sf.
DR InterPro; IPR031768; CBM60_xylan-bd.
DR InterPro; IPR009031; CBM_fam10.
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; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001137; Glyco_hydro_11.
DR InterPro; IPR002509; NODB_dom.
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; PF02013; CBM_10; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM01064; CBM_10; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 1.
DR PROSITE; PS51763; CBM10; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
DR PROSITE; PS50404; GST_NTER; 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:UP000009080};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW ProRule:PRU01097}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..685
FT /note="endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002949065"
FT DOMAIN 35..231
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT DOMAIN 410..587
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 499..587
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 643..671
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT REGION 225..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ SEQUENCE 685 AA; 70232 MW; 5F20CCC524A576D0 CRC64;
MNKNEKRGNY LNSALAAAVL AATATVFTAP VNAQTLTSNS TGTNGGHYYS FWKDSGDASF
TLHSGGRYAS EWNTSTNNWV GGKGWNPGGA KVVNYEGYYG VSNSQNSYLA LYGWTKNPLI
EYYIIESYGS YNPSSCSGGT NYGSFQSDGA TYNVRRCQRV QQPSIEGTAT FYQYFSVRSP
KKGFGQISGT INVGNHFNYW ASQGLNLGSH DYMVLATEGY RSTGSSDISV TEGSAGGSSS
GSSSGGGSSS SGSSSSSSGG NGGAITVRAR GTNGDERISL NVGGSAVASW TLSTSYQNYT
YTGGATGDIQ VEYTNDASGR DVILDYVQVN GETRQAEDME YNTATYANGE CGGGSFSETM
HCSGVIGFGE TSDCFSGSCS GGSSTSSSGG GSSSSSSSGG SSSGGGSCSG YVGITFDDGP
GNYTNTLINA LKTNNLTPVT WFVQGQYIQG NSAAAQQLMS VGEIQNHSWN HPDMTSYSYA
QVVDQISRTT QAIRGAGAPA PTLYRPPYGN NTSAIRQAAQ NQGLRYITWD VDSKDWDGAS
SAQIAAAAGQ MQNGQVILMH DHDYHTRTIN AIPAIASGLR AKGLCAGRID PNTGRAVAPA
GGSSSSSSGG STTSSSSGGS SSSSSGGSSS GSSSSGGTGG SCVCNWWGTN YPVCANSSGW
GWENGQSCIG AQTCNSGGGG GVVCN
//
