XYNB_NEOPA
ID XYNB_NEOPA Reviewed; 860 AA.
AC Q02290;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Endo-1,4-beta-xylanase B;
DE Short=Xylanase B;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE Flags: Precursor;
GN Name=xynB;
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=8172598; DOI=10.1042/bj2990381;
RA Black G.W., Hazlewood G.P., Xue G.P., Orpin C.G., Gilbert H.J.;
RT "Xylanase B from Neocallimastix patriciarum contains a non-catalytic 455-
RT residue linker sequence comprised of 57 repeats of an octapeptide.";
RL Biochem. J. 299:381-387(1994).
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. Hydrolyzes both unsubstituted (oat spelts) and highly
CC substituted (rye and wheat) forms of arabinoxylanslans.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; S71569; AAB30669.1; -; mRNA.
DR PIR; S43846; S43846.
DR AlphaFoldDB; Q02290; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Repeat; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..860
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_0000429666"
FT DOMAIN 21..324
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REPEAT 375..382
FT /note="1"
FT REPEAT 391..398
FT /note="2"
FT REPEAT 415..422
FT /note="3"
FT REPEAT 431..438
FT /note="4"
FT REPEAT 439..446
FT /note="5"
FT REPEAT 447..454
FT /note="6"
FT REPEAT 455..462
FT /note="7"
FT REPEAT 463..470
FT /note="8"
FT REPEAT 471..478
FT /note="9"
FT REPEAT 479..486
FT /note="10"
FT REPEAT 487..494
FT /note="11"
FT REPEAT 495..502
FT /note="12"
FT REPEAT 503..510
FT /note="13"
FT REPEAT 511..518
FT /note="14"
FT REPEAT 519..526
FT /note="15"
FT REPEAT 527..534
FT /note="16"
FT REPEAT 535..542
FT /note="17"
FT REPEAT 543..550
FT /note="18"
FT REPEAT 551..558
FT /note="19"
FT REPEAT 559..566
FT /note="20"
FT REPEAT 567..574
FT /note="21"
FT REPEAT 575..582
FT /note="22"
FT REPEAT 583..590
FT /note="23"
FT REPEAT 591..598
FT /note="24"
FT REPEAT 599..606
FT /note="25"
FT REPEAT 607..614
FT /note="26"
FT REPEAT 615..622
FT /note="27"
FT REPEAT 623..630
FT /note="28"
FT REPEAT 631..638
FT /note="29"
FT REPEAT 639..646
FT /note="30"
FT REPEAT 647..654
FT /note="31"
FT REPEAT 655..662
FT /note="32"
FT REPEAT 663..670
FT /note="33"
FT REPEAT 671..678
FT /note="34"
FT REPEAT 679..686
FT /note="35"
FT REPEAT 687..694
FT /note="36"
FT REPEAT 695..702
FT /note="37"
FT REPEAT 703..710
FT /note="38"
FT REPEAT 711..718
FT /note="39"
FT REPEAT 719..726
FT /note="40"
FT REPEAT 727..734
FT /note="41"
FT REPEAT 735..742
FT /note="42"
FT REPEAT 743..750
FT /note="43"
FT REPEAT 751..758
FT /note="44"
FT REPEAT 759..766
FT /note="45"
FT REPEAT 767..774
FT /note="46"
FT REPEAT 775..782
FT /note="47"
FT DOMAIN 824..860
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 330..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..782
FT /note="47 X 8 AA tandem repeats of [SKN]-S-K-T-L-P-G-G"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 278..284
FT /evidence="ECO:0000250"
SQ SEQUENCE 860 AA; 88052 MW; 677F9032F0A87085 CRC64;
MKFSSANKIL FSGLVASANA YDLLKDYAGD LKIGVAANAM RFSNSNYVNA MKAFNMMVAE
NDCKLSGIQQ QKGVYNFNGC DNHYNKAKEL GMEFRGHCLI WHSYQPSWFQ NADANTLKNA
IVDHITKTLQ HYEGKIKVWD VVNEAIDDNS NGNGWNMRRS FLYNKVPNFV DLAFQTARKV
SPNTKLFYND YNAEGVYAKA ESIYNFVSDL KKRNIPIDGV GLQYHVGAKE QPSYNKINDL
IGRYCKLGLE VHITELDVKL QGDQNGQSQA FSNALKACLA NSCCKAFLVW GVGDNDSWLG
ANEQALLFNG SYQPKPVYNT LLNILKTSAR PASSSAKTLP GNSKSKTLPG VNSKTLPGNK
SKTLPGASKT LPGNKSKTLP GGNSNTLPGN KSKTLPGGNS KTLPGNKSRT LPGGNSKTLP
GGKSRTLPGG NSKTLPGGKS KTLPGGNSKT LPGGKSKTLP GGNSKTLPGG SSKTLPGGKS
KTLPGGNSKT LPGGSSKTLP GGKSKTLPGG SSKTLPGGKS KTLPGGNSKT LPGGNSKTLP
GGSSKTLPGG KSKTLPGGNS KTLPGGSSKT LPGGKSKTLP GGNSKTLPGG NSKTLPGGKS
KTLPGGNSKT LPGGSSKTLP GGKSKTLPGG SSKTLPGGKS KTLPGGNSKT LPGGNSKTLP
GGSSKTLPGG KSKTLPGGSS KTLPGGKSKT LPGGNSKTLP GGKSKTLPGG NSKTLPGGKS
KTLPGGNSKT LPGGKSKTLP GGNSKTLPGG SSKTLPGGKS KTLPGGNSKT LPGGKSKTLP
GGNTKTLPGG ACKPTTVTVT QKVTVTVTVE SQPTQGGMNQ GGGNCAAKWG QCGGNGFNGP
TCCQNGSRCQ FVNEWYSQCL
