XYND_CELFI
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 25-MAY-2022, entry version 126.
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; 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 activity
CC against polysaccharides other than xylan. Hydrolyzes glucosidic bonds
CC with retention of anomeric configuration.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P54865; -.
DR SMR; P54865; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11D_CELFI; -.
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
FT /evidence="ECO:0000255"
FT CHAIN 44..644
FT /note="Bifunctional xylanase/deacetylase"
FT /id="PRO_0000008000"
FT DOMAIN 44..229
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 242..333
FT /note="CBM2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT DOMAIN 356..532
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT DOMAIN 553..644
FT /note="CBM2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 222..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..245
FT /note="Linker ('hinge') (Gly-rich box)"
FT REGION 327..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..350
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 536..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..556
FT /note="Linker ('hinge') (Gly-rich box)"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1E5C"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1E5C"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:1E5B"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1E5B"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1E5B"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1E5B"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1E5C"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:1E5B"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1E5B"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:1HEJ"
FT STRAND 571..579
FT /evidence="ECO:0007829|PDB:1HEH"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:1HEH"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:1HEH"
FT STRAND 609..616
FT /evidence="ECO:0007829|PDB:1HEH"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:1HEH"
FT STRAND 622..629
FT /evidence="ECO:0007829|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
