XYNC_NEOPA
ID XYNC_NEOPA Reviewed; 485 AA.
AC Q9UV68;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, 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 Neocallimastix patriciarum (Rumen fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=4758;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RC STRAIN=27;
RX PubMed=10588045; DOI=10.1139/w99-092;
RA Liu J.H., Selinger B.L., Tsai C.F., Cheng K.J.;
RT "Characterization of a Neocallimastix patriciarum xylanase gene and its
RT product.";
RL Can. J. Microbiol. 45:970-974(1999).
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:10588045}.
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:10588045};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The CBM1 domain is essential for optimal xylanase activity.
CC {ECO:0000269|PubMed:10588045}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; AF123252; AAF14365.1; -; Genomic_DNA.
DR PDB; 3WP4; X-ray; 1.27 A; A=20-244.
DR PDB; 3WP5; X-ray; 1.32 A; A=20-244.
DR PDB; 3WP6; X-ray; 1.43 A; A=20-244.
DR PDBsum; 3WP4; -.
DR PDBsum; 3WP5; -.
DR PDBsum; 3WP6; -.
DR AlphaFoldDB; Q9UV68; -.
DR SMR; Q9UV68; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11C_NEOPA; -.
DR BRENDA; 3.2.1.8; 6834.
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 Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Repeat; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..485
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_0000429667"
FT DOMAIN 34..234
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT REPEAT 275..280
FT /note="1-1"
FT REPEAT 281..286
FT /note="1-2"
FT REPEAT 287..292
FT /note="1-3"
FT REPEAT 293..298
FT /note="1-4"
FT REPEAT 299..304
FT /note="1-5"
FT REPEAT 310..315
FT /note="1-6"
FT REPEAT 316..321
FT /note="1-7"
FT REPEAT 353..361
FT /note="2-1"
FT REPEAT 362..370
FT /note="2-2"
FT REPEAT 371..379
FT /note="2-3"
FT REPEAT 380..388
FT /note="2-4"
FT REPEAT 389..397
FT /note="2-5"
FT REPEAT 399..407
FT /note="2-6"
FT REPEAT 408..416
FT /note="2-7"
FT REPEAT 417..425
FT /note="2-8"
FT DOMAIN 449..484
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 250..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..321
FT /note="7 X 6 AA tandem repeats of G-Q-Q-P-P-Q"
FT REGION 353..425
FT /note="8 X 9 AA tandem repeats of G-G-[SN]-P-W-G-G-N-Q"
FT COMPBIAS 277..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 67..84
FT /evidence="ECO:0007829|PDB:3WP4"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 97..110
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:3WP4"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3WP4"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 174..187
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3WP4"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 212..223
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3WP4"
FT STRAND 229..242
FT /evidence="ECO:0007829|PDB:3WP4"
SQ SEQUENCE 485 AA; 50192 MW; 3FCD43C56DB01E83 CRC64;
MKFLQIIPVL LSLTSTTLAQ SFCSSASHSG QSVKETGNKV GTIGGVGYEL WADSGNNSAT
FYSDGSFSCT FQNAGDYLCR SGLSFDSTKT PSQIGRMKAD FKLVKQNISN VGYSYVGVYG
WTRSPLVEYY IVDNWLSPSP PGDWVGNKKH GSFTIDGAQY TVYENTRTGP SIDGNTTFKQ
YFSIRQQARD CGTIDISAHF DQWEKLGMTM GKLHEAKVLG EAGNGNGGVS GTADFPYAKV
YIGDGNGGGA SPAPAGGAPA GGAPAGNDQP QGPQGQQPPQ GQQPPQGQQP PQGQQPPQGQ
QPPQGNDQQG QQPPQGQQPP QGNDQHQGQH PPQPQGPQGG NPGGSDFNNW SQGGSPWGGN
QGGSPWGGNQ GGNPWGGNQG GSPWGGNQGG SPWGQGNQGG NPWGGNQGGS PWGGNQGGNP
WGGNQWGAPQ NAAAPQSAAA PQNASDGGNC ASLWGQCGGQ GYNGPSCCSE GSCKPINEYF
HQCQK
