XYNA2_THEST
ID XYNA2_THEST Reviewed; 512 AA.
AC P33558;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Endo-1,4-beta-xylanase A;
DE Short=Xylanase A;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE Flags: Precursor;
GN Name=xynA;
OS Thermoclostridium stercorarium (Clostridium stercorarium).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Thermoclostridium.
OX NCBI_TaxID=1510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-40.
RC STRAIN=F-9;
RX PubMed=7763496; DOI=10.1271/bbb.57.273;
RA Sakka K., Kojima Y., Kondo T., Karita S., Ohmiya K., Shimada K.;
RT "Nucleotide sequence of the Clostridium stercorarium xynA gene encoding
RT xylanase A: identification of catalytic and cellulose binding domains.";
RL Biosci. Biotechnol. Biochem. 57:273-277(1993).
RN [2]
RP SEQUENCE REVISION.
RA Sakka K.;
RL Submitted (SEP-1995) 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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Thermostable.;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- DOMAIN: XynA is a modular enzyme. The number of CBM6 (carbohydrate
CC binding type-6) domains varies between strains. The polymeric substrate
CC can interact with several of these CBM6 domains (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; D13325; BAA02584.1; -; Genomic_DNA.
DR AlphaFoldDB; P33558; -.
DR SMR; P33558; -.
DR CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_CLOST; -.
DR UniPathway; UPA00114; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_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; IPR001137; Glyco_hydro_11.
DR Pfam; PF03422; CBM_6; 2.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM00606; CBD_IV; 2.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51175; CBM6; 2.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..512
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000008002"
FT DOMAIN 33..228
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 251..371
FT /note="CBM6 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT REPEAT 279..340
FT /note="1"
FT DOMAIN 388..508
FT /note="CBM6 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT REPEAT 416..477
FT /note="2"
FT REGION 279..477
FT /note="2 X 61 AA approximate repeats"
FT ACT_SITE 124
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 271
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 280
FT /ligand="D-xylobiose"
FT /ligand_id="ChEBI:CHEBI:28309"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 280
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 337
FT /ligand="D-xylobiose"
FT /ligand_id="ChEBI:CHEBI:28309"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 337
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 364
FT /ligand="D-xylobiose"
FT /ligand_id="ChEBI:CHEBI:28309"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 364
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 417
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 474
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 501
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GJ44"
SQ SEQUENCE 512 AA; 55843 MW; 1E133CBF4C139305 CRC64;
MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW KDYGNTIMEL
NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY GCDYNPNGNS YLCVYGWTRN
PLVEYYIVES WGSWRPPGAT PKGTITQWMA GTYEIYETTR VNQPSIDGTA TFQQYWSVRT
SKRTSGTISV TEHFKQWERM GMRMGKMYEV ALTVEGYQSS GYANVYKNEI RIGANPTPAP
SQSPIRRDAF SIIEAEEYNS TNSSTLQVIG TPNNGRGIGY IENGNTVTYS NIDFGSGATG
FSATVATEVN TSIQIRSDSP TGTLLGTLYV SSTGSWNTYQ TVSTNISKIT GVHDIVLVFS
GPVNVDNFIF SRSSPVPAPG DNTRDAYSII QAEDYDSSYG PNLQIFSLPG GGSAIGYIEN
GYSTTYKNID FGDGATSVTA RVATQNATTI QVRLGSPSGT LLGTIYVGST GSFDTYRDVS
ATISNTAGVK DIVLVFSGPV NVDWFVFSKS GT
