XYNA_PHACH
ID XYNA_PHACH Reviewed; 408 AA.
AC Q9HEZ1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 89.
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 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].
RC STRAIN=ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750;
RA Khan S.N., Loera-Corral O., Aspinall T.V., Sims P.F.G.;
RT "Molecular characterization and expression analysis of two endo-1,4-B-
RT xylanase genes from Phanerochaete chrysosporium.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=22783089; DOI=10.4489/myco.2011.39.2.121;
RA Huy N.D., Thiyagarajan S., Son Y.L., Park S.M.;
RT "Heterologous Expression of Endo-1,4-beta-xylanaseA from Phanerochaete
RT chrysosporium in Pichia pastoris.";
RL Mycobiology 39:121-124(2011).
RN [4]
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).
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}.
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:22783089};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 mg/ml for birchwood xylan {ECO:0000269|PubMed:15278289,
CC ECO:0000269|PubMed:22783089};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:15278289,
CC ECO:0000269|PubMed:22783089};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:15278289, ECO:0000269|PubMed:22783089};
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; AF301903; AAG44993.1; -; Genomic_DNA.
DR EMBL; EU302792; ABZ88797.1; -; Genomic_DNA.
DR EMBL; HQ993045; AEK97220.1; -; mRNA.
DR AlphaFoldDB; Q9HEZ1; -.
DR SMR; Q9HEZ1; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR CLAE; XYN10A_PHACH; -.
DR VEuPathDB; FungiDB:AGR57_4281; -.
DR OMA; GIADNHT; -.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..408
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_5000419219"
FT DOMAIN 20..55
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT DOMAIN 88..405
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REGION 64..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 327
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT DISULFID 355..361
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 43571 MW; 4BD5FBD22F6666A0 CRC64;
MKLSASFAAL ALLLPFVQAQ SPVWGQCGGI GWTGPTTCTA GNVCQEYSAY YSQCIPASQA
TSVTSVSTAP NPPPTSHTST SSAPSGASTS TAKLNTLAKA KGKLYFGTAT DNGELSDTAY
TAILDDNTMF GQITPANSMK WDATEPQQGQ FTFSGGDQIA NLAKSNGMLL RGHNCVWYNQ
LPSWVSNGKF TAAQLTSIIQ NHCSTLVTHY KGQVYAWDVV NEPFNDDGSW RTDVFYNTLG
TSYVQIALEA ARAADPDAKL YINEYNIEYA GAKATSLLNL VKTLKAASVP LDGIGFQSHF
IVGQVPTGLQ SQLTTFAAQG VEVAITELDI RMTLPSTPAL LAQQKTDYSN VIKACASVEA
CVGVTVWDWT DKYSWVPNTF SGQGAACPWD QNFVRKPAYD GIAIGFGN
