XYNA_NEOPA
ID XYNA_NEOPA Reviewed; 607 AA.
AC P29127;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Bifunctional endo-1,4-beta-xylanase A;
DE Short=XYLA;
DE EC=3.2.1.8;
DE Flags: Precursor;
GN Name=XYNA;
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].
RX PubMed=1406248; DOI=10.1111/j.1365-2958.1992.tb01379.x;
RA Gilbert H.J., Hazlewood G.P., Laurie J.I., Orpin C.G., Xue G.P.;
RT "Homologous catalytic domains in a rumen fungal xylanase: evidence for gene
RT duplication and prokaryotic origin.";
RL Mol. Microbiol. 6:2065-2072(1992).
CC -!- FUNCTION: Hydrolyzes xylans into xylobiose and xylose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; X65526; CAA46498.1; -; mRNA.
DR PIR; S24754; S24754.
DR PDB; 2C1F; X-ray; 2.10 A; A=275-499.
DR PDB; 2VG9; X-ray; 2.00 A; A=275-492.
DR PDBsum; 2C1F; -.
DR PDBsum; 2VG9; -.
DR AlphaFoldDB; P29127; -.
DR SMR; P29127; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_NEOPA; -.
DR BRENDA; 3.2.1.8; 6834.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P29127; -.
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; -; 2.
DR Gene3D; 3.90.1220.10; -; 2.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR009034; Dockerin_dom_fun_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033119; GH11_AS_2.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF02013; CBM_10; 2.
DR Pfam; PF00457; Glyco_hydro_11; 2.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF64571; SSF64571; 2.
DR PROSITE; PS51763; CBM10; 2.
DR PROSITE; PS00776; GH11_1; 2.
DR PROSITE; PS00777; GH11_2; 2.
DR PROSITE; PS51761; GH11_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Multifunctional enzyme; Polysaccharide degradation; Repeat; Signal;
KW Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..607
FT /note="Bifunctional endo-1,4-beta-xylanase A"
FT /id="PRO_0000008016"
FT DOMAIN 35..242
FT /note="GH11 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 280..487
FT /note="GH11 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 523..563
FT /note="CBM10 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT DOMAIN 566..606
FT /note="CBM10 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT REGION 248..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 474
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:2VG9"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 345..375
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 385..395
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 410..423
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 426..440
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:2VG9"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:2VG9"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:2VG9"
FT STRAND 468..492
FT /evidence="ECO:0007829|PDB:2VG9"
SQ SEQUENCE 607 AA; 66175 MW; 9C5B73A67D0CC780 CRC64;
MRTIKFFFAV AIATVAKAQW GGGGASAGQR LTVGNGQTQH KGVADGYSYE IWLDNTGGSG
SMTLGSGATF KAEWNASVNR GNFLARRGLD FGSQKKATDY SYIGLDYTAT YRQTGSASGN
SRLCVYGWFQ NRGVQGVPLV EYYIIEDWVD WVSDAQGRMV TIDGAQYKIF QMDHTGPTIN
GGSETFKQYF SVRQQKRTSG HITVSDHFKE WAKQGWGIGN LYEVALNAEG WQSSGIADVT
KLDVYTTQKG SNPAPTSTGT VPSSSAGGST ANGKKFTVGN GQNQHKGVND GFSYEIWLDN
TGGNGSMTLG SGATFKAEWN AAVNRGNFLA RRGLDFGSQK KATDYDYIGL DYAATYKQTA
SASGNSRLCV YGWFQNRGLN GVPLVEYYII EDWVDWVPDA QGKMVTIDGA QYKIFQMDHT
GPTINGGSET FKQYFSVRQQ KRTSGHITVS DHFKEWAKQG WGIGNLYEVA LNAEGWQSSG
VADVTLLDVY TTPKGSSPAT SAAPRTTTRT TTRTKSLPTN YNKCSARITA QGYKCCSDPN
CVVYYTDEDG TWGVENNDWC GCGVEQCSSK ITSQGYKCCS DPNCVVFYTD DDGKWGVENN
DWCGCGF
