XYNC_TALFU
ID XYNC_TALFU Reviewed; 223 AA.
AC Q9HFH0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 84.
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 Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium
OS funiculosum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=28572;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=12147340; DOI=10.1016/s0167-4838(02)00366-7;
RA Furniss C.S., Belshaw N.J., Alcocer M.J., Williamson G., Elliott G.O.,
RA Gebruers K., Haigh N.P., Fish N.M., Kroon P.A.;
RT "A family 11 xylanase from Penicillium funiculosum is strongly inhibited by
RT three wheat xylanase inhibitors.";
RL Biochim. Biophys. Acta 1598:24-29(2002).
RN [2]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=17216454; DOI=10.1007/s00253-006-0764-0;
RA Berrin J.G., Ajandouz el H., Georis J., Arnaut F., Juge N.;
RT "Substrate and product hydrolysis specificity in family 11 glycoside
RT hydrolases: an analysis of Penicillium funiculosum and Penicillium
RT griseofulvum xylanases.";
RL Appl. Microbiol. Biotechnol. 74:1001-1010(2007).
RN [3] {ECO:0007744|PDB:1TE1}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 34-223 IN COMPLEX WITH INHIBITOR
RP XIP-I.
RX PubMed=15181003; DOI=10.1074/jbc.m404225200;
RA Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G.,
RA Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A.;
RT "The dual nature of the wheat xylanase protein inhibitor XIP-I: structural
RT basis for the inhibition of family 10 and family 11 xylanases.";
RL J. Biol. Chem. 279:36029-36037(2004).
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.
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:12147340,
CC ECO:0000269|PubMed:17216454};
CC -!- ACTIVITY REGULATION: Strongly inhibited by wheat xylanase inhibiting
CC protein I (XIP-I), and by proteinaceous endoxylanase Triticum aestivum
CC xylanase inhibitors I and II (TAXI-I and TAXI-II).
CC {ECO:0000269|PubMed:12147340, ECO:0000269|PubMed:17216454}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=2540 umol/min/mg enzyme toward birchwood xylan at pH 5.5 and 30
CC degrees Celsius {ECO:0000269|PubMed:12147340,
CC ECO:0000269|PubMed:17216454};
CC Vmax=7190 umol/min/mg enzyme toward soluble wheat arabinoxylans at pH
CC 5.5 and 30 degrees Celsius {ECO:0000269|PubMed:12147340,
CC ECO:0000269|PubMed:17216454};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:12147340,
CC ECO:0000269|PubMed:17216454};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:12147340, ECO:0000269|PubMed:17216454};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBUNIT: Interacts directly with the wheat xylanase inhibiting protein
CC I (XIP-I). {ECO:0000269|PubMed:15181003}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12147340}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; AJ278385; CAC15487.1; -; Genomic_DNA.
DR PDB; 1TE1; X-ray; 2.50 A; B=34-223.
DR PDB; 3WP3; X-ray; 1.98 A; A/B=28-223.
DR PDBsum; 1TE1; -.
DR PDBsum; 3WP3; -.
DR AlphaFoldDB; Q9HFH0; -.
DR SMR; Q9HFH0; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11C_PENFN; -.
DR BRENDA; 3.2.1.8; 4616.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; Q9HFH0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..223
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_5000066092"
FT DOMAIN 35..223
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT REGION 5..7
FT /note="Interaction with protein inhibitor XIP-I"
FT /evidence="ECO:0000269|PubMed:15181003"
FT REGION 18..23
FT /note="Interaction with protein inhibitor XIP-I"
FT /evidence="ECO:0000269|PubMed:15181003"
FT REGION 85..87
FT /note="Interaction with protein inhibitor XIP-I"
FT /evidence="ECO:0000269|PubMed:15181003"
FT REGION 123..130
FT /note="Interaction with protein inhibitor XIP-I"
FT /evidence="ECO:0000269|PubMed:15181003"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 44
FT /note="Interaction with protein inhibitor XIP-I"
FT /evidence="ECO:0000269|PubMed:15181003"
FT SITE 170
FT /note="Interaction with protein inhibitor XIP-I"
FT /evidence="ECO:0000269|PubMed:15181003"
FT SITE 176
FT /note="Interaction with protein inhibitor XIP-I"
FT /evidence="ECO:0000269|PubMed:15181003"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 92..114
FT /evidence="ECO:0007829|PDB:3WP3"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:3WP3"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 163..176
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:3WP3"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 201..213
FT /evidence="ECO:0007829|PDB:3WP3"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:3WP3"
SQ SEQUENCE 223 AA; 24045 MW; 428CD224C8F13C77 CRC64;
MKLFLAAIVL CATAATAFPS ELAQRAAGDL SKRQSITTSQ TGTNNGYYYS FWTNGGGEVT
YTNGDNGEYS VTWVDCGDFT SGKGWNPANA QTVTYSGEFN PSGNAYLAVY GWTTDPLVEY
YILESYGTYN PSSGLTSLGQ VTSDGGTYDI YSTQRVNQPS IEGTSTFNQY WSVRTEKRVG
GTVTTANHFA AWKALGLEMG TYNYMIVSTE GYESSGSSTI TVS
