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Database: UniProt
Entry: P54865
LinkDB: P54865
Original site: P54865 
ID   XYND_CELFI              Reviewed;         644 AA.
AC   P54865;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-DEC-2018, entry version 117.
DE   RecName: Full=Bifunctional xylanase/deacetylase;
DE   Includes:
DE     RecName: Full=Endo-1,4-beta-xylanase D;
DE              Short=XYLD;
DE              Short=Xylanase D;
DE              EC=3.2.1.8;
DE   Includes:
DE     RecName: Full=Acetylated xylan deacetylase;
DE              EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=xynD;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=221;
RX   PubMed=8170399; DOI=10.1111/j.1365-2958.1994.tb00317.x;
RA   Millward-Sadler S.J., Poole D.M., Henrissat B., Hazlewood G.P.,
RA   Clarke J.H., Gilbert H.J.;
RT   "Evidence for a general role for high-affinity non-catalytic cellulose
RT   binding domains in microbial plant cell wall hydrolases.";
RL   Mol. Microbiol. 11:375-382(1994).
CC   -!- FUNCTION: Endo-acting xylanase which displays no detectable
CC       activity against polysaccharides other than xylan. Hydrolyzes
CC       glucosidic bonds with retention of anomeric configuration.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; X76729; CAA54145.1; -; Genomic_DNA.
DR   PIR; I40712; I40712.
DR   PDB; 1E5B; NMR; -; A=247-333.
DR   PDB; 1E5C; NMR; -; A=247-333.
DR   PDB; 1HEH; NMR; -; C=557-644.
DR   PDB; 1HEJ; NMR; -; C=557-644.
DR   PDB; 1XBD; NMR; -; A=247-333.
DR   PDB; 2XBD; NMR; -; A=247-333.
DR   PDBsum; 1E5B; -.
DR   PDBsum; 1E5C; -.
DR   PDBsum; 1HEH; -.
DR   PDBsum; 1HEJ; -.
DR   PDBsum; 1XBD; -.
DR   PDBsum; 2XBD; -.
DR   ProteinModelPortal; P54865; -.
DR   SMR; P54865; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11D_CELFI; -.
DR   PRIDE; P54865; -.
DR   eggNOG; ENOG4107T94; Bacteria.
DR   eggNOG; ENOG410YH6C; LUCA.
DR   BRENDA; 3.2.1.8; 1233.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P54865; -.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.40.290; -; 2.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
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; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00637; CBD_II; 2.
DR   SUPFAM; SSF49384; SSF49384; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS51173; CBM2; 2.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS51677; NODB; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Multifunctional enzyme; Polysaccharide degradation; Repeat; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     43       {ECO:0000255}.
FT   CHAIN        44    644       Bifunctional xylanase/deacetylase.
FT                                /FTId=PRO_0000008000.
FT   DOMAIN       44    229       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      242    333       CBM2 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01135}.
FT   DOMAIN      356    532       NodB homology. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01014}.
FT   DOMAIN      553    644       CBM2 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01135}.
FT   REGION      231    245       Linker ("hinge") (Gly-rich box).
FT   REGION      337    350       Linker ("hinge") (Pro-Thr box).
FT   REGION      548    556       Linker ("hinge") (Gly-rich box).
FT   COMPBIAS    231    238       Poly-Gly.
FT   ACT_SITE    126    126       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    216    216       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   STRAND      250    252       {ECO:0000244|PDB:1E5C}.
FT   STRAND      255    258       {ECO:0000244|PDB:1E5C}.
FT   STRAND      260    268       {ECO:0000244|PDB:1E5B}.
FT   STRAND      278    280       {ECO:0000244|PDB:1E5B}.
FT   STRAND      287    293       {ECO:0000244|PDB:1E5B}.
FT   STRAND      296    300       {ECO:0000244|PDB:1E5B}.
FT   STRAND      302    304       {ECO:0000244|PDB:1E5C}.
FT   STRAND      311    318       {ECO:0000244|PDB:1E5B}.
FT   STRAND      327    329       {ECO:0000244|PDB:1E5B}.
FT   STRAND      562    565       {ECO:0000244|PDB:1HEJ}.
FT   STRAND      571    579       {ECO:0000244|PDB:1HEH}.
FT   STRAND      589    591       {ECO:0000244|PDB:1HEH}.
FT   STRAND      601    607       {ECO:0000244|PDB:1HEH}.
FT   STRAND      609    616       {ECO:0000244|PDB:1HEH}.
FT   STRAND      618    620       {ECO:0000244|PDB:1HEH}.
FT   STRAND      622    629       {ECO:0000244|PDB:1HEH}.
SQ   SEQUENCE   644 AA;  66582 MW;  56B045CC6E0E1820 CRC64;
     MSDSFEATRT TRRRRPLQAL TGLLAAGALV AGALAAASPA AAAVTSNTTG THDGYFYSFW
     TDSPGSVSMD LNSGGGYTRW SNTGNFVAGK GWSTGGRKTV SYSGQFNPSR NAYLTLYGWT
     QSPLVEYYIV DSWGTYRPTG TFMGTVTSDG GTYDIYRTQR VNKPSIEGDS STFYQYWSVR
     QQKRTGGTIT SGNHFDAWAS KGMNLGRHNY MIMATEGYQS SGSSSITVSE GSGGGGGGDT
     GGGGGSTGCS VTATRAEEWS DRFNVTYSVS GSSAWTVNLA LNGSQTIQAS WNANVTGSGS
     TRTVTPNGSG NTFGVTVMKN GSSTTPAATC AGSGGGTATP TPTPTPTPTP QSCSAGYVGL
     TFDDGPNTGT TNQILSTLTQ YGATATVFPT GQNAQGNPSL MQAYKNAGVQ IGNHSWDHPH
     LVNMSQSDMQ SQLTRTQQAI QQTAGVTPTL FRPPYGESNA TLRQVESSLG LREIIWDVDS
     QDWNNASASQ IRQAASRLTN GQIILMHDWP AATVQALPGI LQDLRSRNLC TGHISSSTGR
     AVAPSSAGGG GGGGGGTGSC SVSAVRGEEW ADRFNVTYSV SGSSSWVVTL GLNGGQSVQS
     SWNAALTGSS GTVTARPNGS GNSFGVTFYK NGSSATPGAT CATG
//
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