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Database: UniProt
Entry: O69230
LinkDB: O69230
Original site: O69230 
ID   XYNC_PAEBA              Reviewed;        1086 AA.
AC   O69230;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   12-SEP-2018, entry version 88.
DE   RecName: Full=Endo-1,4-beta-xylanase C;
DE            Short=Xylanase C;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase C;
DE   Flags: Precursor;
GN   Name=xynC;
OS   Paenibacillus barcinonensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=198119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=10463183; DOI=10.1099/13500872-145-8-2163;
RA   Blanco A., Diaz P., Zueco J., Parascandola P., Pastor F.I.J.;
RT   "A multidomain xylanase from a Bacillus sp. with a region homologous
RT   to thermostabilizing domains of thermophilic enzymes.";
RL   Microbiology 145:2163-2170(1999).
CC   -!- FUNCTION: Endoxylanase with high hydrolytic activity on birchwood
CC       and oat spelt xylan. Xylotetraose, xylotriose, xylobiose and
CC       xylose are the main products from birchwood xylan hydrolysis.
CC       Shows increasing activity on xylo-oligosaccharides of increasing
CC       length. Displays very low hydrolytic activity on Avicel,
CC       carboxymethylcellulose (CMC) and p-nitrophenyl-beta-
CC       xylopyranoside. Also shows transxylosidase activity, allowing the
CC       formation of xylo-oligosaccharides of higher degreee of
CC       polymerization than the starting substrate.
CC       {ECO:0000269|PubMed:10463183}.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans. {ECO:0000269|PubMed:10463183}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5. Retains at least 50% of its maximum activity
CC         between pH 4.5 and 8.0. Is not active at pH values below 4.5,
CC         while at least 35% of maximum activity is found in the pH range
CC         8.5-11.0. {ECO:0000269|PubMed:10463183};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Is only stable at 55
CC         degrees Celsius or lower temperatures. Retains more than 77%
CC         activity after 2 hours incubation at 55 degrees Celsius and pH
CC         7. {ECO:0000269|PubMed:10463183};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- DOMAIN: Consists of three different domains. The central region of
CC       the enzyme is the catalytic domain. The N-terminal region contains
CC       cenC-type cellulose-binding domains and seems to act as a
CC       thermostabilizing domain: a derivative lacking this region shows a
CC       lower optimum temperature for activity (35 degrees Celsius) than
CC       the full-length enzyme, and a reduced thermal stability that
CC       results in a complete inactivation of the enzyme after 2 hours
CC       incubation at 55 degrees Celsius. The C-terminal region contains
CC       family 9 carbohydrate-binding modules.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
DR   EMBL; AJ006645; CAA07173.1; -; Genomic_DNA.
DR   PIR; T17628; T17628.
DR   PDB; 4W8L; X-ray; 1.76 A; A/B/C=367-718.
DR   PDB; 4XUN; X-ray; 1.75 A; A/B/C=186-366.
DR   PDB; 4XUO; X-ray; 1.70 A; A/B=29-186.
DR   PDB; 4XUP; X-ray; 2.43 A; A/B/C/D/E/F=28-361.
DR   PDB; 4XUQ; X-ray; 1.95 A; A/B/C=186-366.
DR   PDB; 4XUR; X-ray; 1.67 A; A/B/C=186-366.
DR   PDB; 4XUT; X-ray; 1.80 A; A/B/C=186-366.
DR   PDBsum; 4W8L; -.
DR   PDBsum; 4XUN; -.
DR   PDBsum; 4XUO; -.
DR   PDBsum; 4XUP; -.
DR   PDBsum; 4XUQ; -.
DR   PDBsum; 4XUR; -.
DR   PDBsum; 4XUT; -.
DR   ProteinModelPortal; O69230; -.
DR   SMR; O69230; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   PRIDE; O69230; -.
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:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06452; CBM9_1; 2.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32   1086       Endo-1,4-beta-xylanase C.
FT                                /FTId=PRO_0000371420.
FT   DOMAIN       35    183       CBM-cenC 1.
FT   DOMAIN      197    359       CBM-cenC 2.
FT   DOMAIN      365    710       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    502    502       Proton donor. {ECO:0000250}.
FT   ACT_SITE    556    556       {ECO:0000250}.
FT   ACT_SITE    620    620       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10061}.
FT   STRAND       37     41       {ECO:0000244|PDB:4XUO}.
FT   STRAND       45     47       {ECO:0000244|PDB:4XUO}.
FT   STRAND       52     56       {ECO:0000244|PDB:4XUO}.
FT   STRAND       58     64       {ECO:0000244|PDB:4XUO}.
FT   STRAND       67     70       {ECO:0000244|PDB:4XUO}.
FT   STRAND       72     76       {ECO:0000244|PDB:4XUO}.
FT   STRAND       84     88       {ECO:0000244|PDB:4XUO}.
FT   TURN         90     92       {ECO:0000244|PDB:4XUO}.
FT   STRAND       98    107       {ECO:0000244|PDB:4XUO}.
FT   STRAND      114    123       {ECO:0000244|PDB:4XUO}.
FT   STRAND      129    133       {ECO:0000244|PDB:4XUO}.
FT   STRAND      138    140       {ECO:0000244|PDB:4XUO}.
FT   STRAND      142    144       {ECO:0000244|PDB:4XUO}.
FT   STRAND      146    152       {ECO:0000244|PDB:4XUO}.
FT   STRAND      158    168       {ECO:0000244|PDB:4XUO}.
FT   STRAND      173    184       {ECO:0000244|PDB:4XUO}.
FT   STRAND      201    203       {ECO:0000244|PDB:4XUR}.
FT   STRAND      216    218       {ECO:0000244|PDB:4XUR}.
FT   STRAND      220    226       {ECO:0000244|PDB:4XUR}.
FT   STRAND      229    238       {ECO:0000244|PDB:4XUR}.
FT   STRAND      248    250       {ECO:0000244|PDB:4XUR}.
FT   HELIX       252    254       {ECO:0000244|PDB:4XUR}.
FT   STRAND      260    268       {ECO:0000244|PDB:4XUR}.
FT   STRAND      271    286       {ECO:0000244|PDB:4XUR}.
FT   STRAND      294    304       {ECO:0000244|PDB:4XUR}.
FT   STRAND      309    316       {ECO:0000244|PDB:4XUR}.
FT   HELIX       320    322       {ECO:0000244|PDB:4XUR}.
FT   STRAND      324    332       {ECO:0000244|PDB:4XUR}.
FT   HELIX       338    340       {ECO:0000244|PDB:4XUR}.
FT   HELIX       344    346       {ECO:0000244|PDB:4XUR}.
FT   STRAND      349    358       {ECO:0000244|PDB:4XUR}.
FT   HELIX       371    375       {ECO:0000244|PDB:4W8L}.
FT   STRAND      378    385       {ECO:0000244|PDB:4W8L}.
FT   HELIX       387    390       {ECO:0000244|PDB:4W8L}.
FT   HELIX       395    403       {ECO:0000244|PDB:4W8L}.
FT   STRAND      405    411       {ECO:0000244|PDB:4W8L}.
FT   HELIX       415    418       {ECO:0000244|PDB:4W8L}.
FT   HELIX       428    439       {ECO:0000244|PDB:4W8L}.
FT   STRAND      443    447       {ECO:0000244|PDB:4W8L}.
FT   STRAND      452    454       {ECO:0000244|PDB:4W8L}.
FT   HELIX       457    460       {ECO:0000244|PDB:4W8L}.
FT   HELIX       472    490       {ECO:0000244|PDB:4W8L}.
FT   TURN        491    493       {ECO:0000244|PDB:4W8L}.
FT   STRAND      496    501       {ECO:0000244|PDB:4W8L}.
FT   STRAND      508    510       {ECO:0000244|PDB:4W8L}.
FT   HELIX       513    515       {ECO:0000244|PDB:4W8L}.
FT   HELIX       519    523       {ECO:0000244|PDB:4W8L}.
FT   HELIX       534    546       {ECO:0000244|PDB:4W8L}.
FT   STRAND      551    558       {ECO:0000244|PDB:4W8L}.
FT   TURN        559    561       {ECO:0000244|PDB:4W8L}.
FT   HELIX       563    578       {ECO:0000244|PDB:4W8L}.
FT   STRAND      585    588       {ECO:0000244|PDB:4W8L}.
FT   STRAND      591    593       {ECO:0000244|PDB:4W8L}.
FT   HELIX       599    610       {ECO:0000244|PDB:4W8L}.
FT   TURN        611    613       {ECO:0000244|PDB:4W8L}.
FT   STRAND      615    631       {ECO:0000244|PDB:4W8L}.
FT   HELIX       638    659       {ECO:0000244|PDB:4W8L}.
FT   TURN        660    662       {ECO:0000244|PDB:4W8L}.
FT   STRAND      664    670       {ECO:0000244|PDB:4W8L}.
FT   HELIX       674    676       {ECO:0000244|PDB:4W8L}.
FT   HELIX       678    680       {ECO:0000244|PDB:4W8L}.
FT   STRAND      682    684       {ECO:0000244|PDB:4W8L}.
FT   STRAND      692    694       {ECO:0000244|PDB:4W8L}.
FT   HELIX       702    708       {ECO:0000244|PDB:4W8L}.
FT   HELIX       710    712       {ECO:0000244|PDB:4W8L}.
SQ   SEQUENCE   1086 AA;  120586 MW;  4378361F1801A326 CRC64;
     MRGKWLRLCL AAVLIVSLLP GLGAGEWKAS AAKAGDILLS HSFEEGTTQG WTARGGVKVD
     VTAEQAYQGK QSLQTTGRTE AWNGPSLSLT DVVHKNEVVE ISGYVKLVAG SAPPDLKFTV
     ERRDRNGDTQ YDQVNAAEQV TDQKWVKLQG QYSYEQGSSL LLYLESTDAK AAYLLDEFQI
     RLVKAAPENP GEPGEAGQAL FKAYFEDGNI GNWRARGTEK LEVVSGIGHN SNRSLKTSSR
     SETYHGPLVE VLPYLQKGST VHISFWAMYD EGPATQVING SLEKEFNRDT ANLEYAMFAS
     TTLNKGQWKK IEADIIVPAE STGISGLRMY AETPWKQSSE VTETDTIPFY VDDVQITATE
     AIAIEKNIPD LAKKLGSSYA LGAAIDQTAL DPKDPHSELL TKHFNSITAG NFMKMDAMQP
     TEGKFVWSEA DKLVNFAAAN NMQVRGHTLL WHSQVPDWFF TDPNDPSKPA TREQLMQRMK
     THIQTIVSRY KGKVHTWDVV NEVISDGGGL RNQASGSKWR DIIGDVDGDG DDSDYIELAF
     RYAREADPDA VLVINDYGIE GSVSKMNDMV KLVEKLLAKG TPIDAIGFQM HVSMYGPDIK
     QIREAFNRAA ALGVHIQVTE LDMSIYSGNS EQEKPVTDEM MLEQAYRYRA LFDLFKEFDD
     RGVMDSVTLW GLADDGTWLD DFPVKGRKDA PLLFDRKLKA KPAYWALVDP STLPVYRNEW
     TASQAKVSLP DRKGQEDIIW GAVRALPFSH VIEGAVGTTG EVKTLWDGKQ LNLRIEVKDA
     TRLKGDQVEV FVSPEDMTAG KKNSTPKDGQ YIFNRDGGKG KDQKLYQVKE NKSGYVVYAS
     LPLSSADLAA GKVLSLDFRI TDKQPNGKTS IVVWNDVNNQ QPQKTENRGK LKLGFDLKHA
     KVMYGTPTVD GKEDKLWKKA VTITTDVKVT GNSGAKAKAK LLWDEKYLYV LAEVKDPLLS
     KKSANAHEQD SIELFIDLNK NQTNSYEEDD AQYRVNFDNE TSFGGSPRKE LFKSATRLTK
     EGYIVEAAIP LENVRTKESK WIGFDLQVND DGAGDGKRSS VFMWSDPSGN SYRDTSGFGS
     LLLMKK
//
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