XYNC_PHACH
ID XYNC_PHACH Reviewed; 399 AA.
AC B7SIW2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 54.
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 Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, IDENTIFICATION BY
RP MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=RP78;
RX PubMed=15278289; DOI=10.1007/s00294-004-0520-x;
RA Decelle B., Tsang A., Storms R.K.;
RT "Cloning, functional expression and characterization of three Phanerochaete
RT chrysosporium endo-1,4-beta-xylanases.";
RL Curr. Genet. 46:166-175(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16348798; DOI=10.1128/aem.58.11.3466-3471.1992;
RA Dobozi M.S., Szakacs G., Bruschi C.V.;
RT "Xylanase Activity of Phanerochaete chrysosporium.";
RL Appl. Environ. Microbiol. 58:3466-3471(1992).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23361183; DOI=10.1007/s00449-013-0891-9;
RA Huy N.D., Thiyagarajan S., Choi Y.E., Kim D.H., Park S.M.;
RT "Cloning and characterization of a thermostable endo-arabinanase from
RT Phanerochaete chrysosporium and its synergistic action with endo-
RT xylanase.";
RL Bioprocess Biosyst. Eng. 36:677-685(2013).
CC -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. {ECO:0000269|PubMed:15278289,
CC ECO:0000269|PubMed:16348798, ECO:0000269|PubMed:23361183}.
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:15278289,
CC ECO:0000269|PubMed:16348798, ECO:0000269|PubMed:23361183};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.71 mg/ml for birchwood xylan {ECO:0000269|PubMed:15278289};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:15278289};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:15278289};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15278289}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; EU302794; ABZ88799.1; -; Genomic_DNA.
DR AlphaFoldDB; B7SIW2; -.
DR SMR; B7SIW2; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR CLAE; XYN10C_PHACH; -.
DR VEuPathDB; FungiDB:AGR57_8937; -.
DR OMA; GQDYISI; -.
DR UniPathway; UPA00114; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose 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; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00236; fCBD; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..399
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_5000419221"
FT DOMAIN 21..56
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT DOMAIN 81..396
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT DISULFID 346..352
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 42340 MW; 6EBD670479BA3A93 CRC64;
MFKFSASLAA LAALVPFVAA QSPEWGQCGG IGWTGPTTCV AGTTCVESNP YYSQCLPGAA
SVAPPPPSGT SSAGGSTPSS SAKLHTLAKA AGKLYFGTAT DNNELTDTAY TAILDDNTMF
GQITPANSMK WDATEPQQGV FTFSGGDQIA TLAKTNGMLL RGHNCVWYNQ LPSWVSSGSF
TAAQLTSIIQ NHCSTLVTHY KGQVYAWDVV NEPFNDDGTW RTDVFYNTLG TSYVQIALEA
ARAADPNAKL YINEYNIEFA GAKATSLLNL VKSLKAADVP LDGIGFQCHL IVGEFSGPGL
QTQLSTFAAQ GVEVAITELD IRMTLPSTPA LLAQQQTDYN SVITACMNVE SCIGVTVWDW
TDKYSWVPNT FSGQGAACPW DQNFVKKPAF NGIAAGFSA
