XYNC_PAEBA
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 03-AUG-2022, entry version 98.
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; Paenibacillus.
OX NCBI_TaxID=198119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL 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 to
RT thermostabilizing domains of thermophilic enzymes.";
RL Microbiology 145:2163-2170(1999).
CC -!- FUNCTION: Endoxylanase with high hydrolytic activity on birchwood and
CC oat spelt xylan. Xylotetraose, xylotriose, xylobiose and xylose are the
CC main products from birchwood xylan hydrolysis. Shows increasing
CC activity on xylo-oligosaccharides of increasing length. Displays very
CC low hydrolytic activity on Avicel, carboxymethylcellulose (CMC) and p-
CC nitrophenyl-beta-xylopyranoside. Also shows transxylosidase activity,
CC allowing the formation of xylo-oligosaccharides of higher degree of
CC polymerization than the starting substrate.
CC {ECO:0000269|PubMed:10463183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:10463183};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. Retains at least 50% of its maximum activity between
CC pH 4.5 and 8.0. Is not active at pH values below 4.5, while at least
CC 35% of maximum activity is found in the pH range 8.5-11.0.
CC {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% activity
CC after 2 hours incubation at 55 degrees Celsius and pH 7.
CC {ECO:0000269|PubMed:10463183};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- DOMAIN: Consists of three different domains. The central region of the
CC enzyme is the catalytic domain. The N-terminal region contains cenC-
CC type cellulose-binding domains and seems to act as a thermostabilizing
CC domain: a derivative lacking this region shows a lower optimum
CC temperature for activity (35 degrees Celsius) than the full-length
CC enzyme, and a reduced thermal stability that results in a complete
CC inactivation of the enzyme after 2 hours incubation at 55 degrees
CC Celsius. The C-terminal region contains family 9 carbohydrate-binding
CC modules.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; 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 UniPathway; UPA00114; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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 InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
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
FT /evidence="ECO:0000255"
FT CHAIN 32..1086
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_0000371420"
FT DOMAIN 35..183
FT /note="CBM-cenC 1"
FT DOMAIN 197..359
FT /note="CBM-cenC 2"
FT DOMAIN 365..710
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 556
FT /evidence="ECO:0000250"
FT ACT_SITE 620
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4XUO"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 158..168
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:4XUO"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:4XUR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 271..286
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 294..304
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:4XUR"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:4XUR"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:4XUR"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4XUR"
FT STRAND 349..358
FT /evidence="ECO:0007829|PDB:4XUR"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 428..439
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 472..490
FT /evidence="ECO:0007829|PDB:4W8L"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 519..523
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 534..546
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 551..558
FT /evidence="ECO:0007829|PDB:4W8L"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 563..578
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 599..610
FT /evidence="ECO:0007829|PDB:4W8L"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 615..631
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 638..659
FT /evidence="ECO:0007829|PDB:4W8L"
FT TURN 660..662
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 664..670
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:4W8L"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 702..708
FT /evidence="ECO:0007829|PDB:4W8L"
FT HELIX 710..712
FT /evidence="ECO:0007829|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
