ID XYNY_ACETH Reviewed; 1077 AA. AC P51584; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 03-MAY-2023, entry version 141. DE RecName: Full=Endo-1,4-beta-xylanase Y; DE Short=Xylanase Y; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase Y; DE Short=XylY; DE Flags: Precursor; GN Name=xynY; OS Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium OS thermocellum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=1515; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=YS; RX PubMed=7717969; DOI=10.1042/bj3070151; RA Fontes C.M.G.A., Hazelwood G.P., Morag E., Hall J., Hirst B.H., RA Gilbert H.J.; RT "Evidence for a general role for non-catalytic thermostabilizing domains in RT xylanases from thermophilic bacteria."; RL Biochem. J. 307:151-158(1995). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.8.; CC Temperature dependence: CC Optimum temperature is 75 degrees Celsius.; CC -!- INTERACTION: CC P51584; Q06851: cipA; Xeno; NbExp=5; IntAct=EBI-1037473, EBI-687595; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X83269; CAA58242.1; -; Genomic_DNA. DR PIR; S54975; S54975. DR PDB; 1DYO; X-ray; 2.10 A; A/B=558-718. DR PDB; 1GKK; X-ray; 1.60 A; A/B=792-1077. DR PDB; 1GKL; X-ray; 1.40 A; A/B=792-1077. DR PDB; 1H6X; X-ray; 2.23 A; A=560-720. DR PDB; 1H6Y; X-ray; 2.12 A; A/B=560-720. DR PDB; 1OHZ; X-ray; 2.20 A; B=733-791. DR PDB; 1WB4; X-ray; 1.40 A; A/B=792-1077. DR PDB; 1WB5; X-ray; 1.40 A; A/B=792-1077. DR PDB; 1WB6; X-ray; 1.40 A; A/B=792-1077. DR PDB; 2CCL; X-ray; 2.03 A; B/D=730-791. DR PDB; 2W5F; X-ray; 1.90 A; A/B=32-551. DR PDB; 2WYS; X-ray; 2.75 A; A/B=33-551. DR PDB; 2WZE; X-ray; 2.50 A; A/B=33-551. DR PDB; 3ZI7; X-ray; 2.30 A; A/B=792-1077. DR PDB; 4BAG; X-ray; 1.90 A; A/B=792-1077. DR PDB; 4H35; X-ray; 1.90 A; A/B=792-1077. DR PDB; 5FXM; X-ray; 1.99 A; A=792-1077. DR PDB; 6FJ4; X-ray; 1.70 A; A=803-1077. DR PDB; 6Y8G; X-ray; 1.80 A; AAA/BBB=792-1077. DR PDBsum; 1DYO; -. DR PDBsum; 1GKK; -. DR PDBsum; 1GKL; -. DR PDBsum; 1H6X; -. DR PDBsum; 1H6Y; -. DR PDBsum; 1OHZ; -. DR PDBsum; 1WB4; -. DR PDBsum; 1WB5; -. DR PDBsum; 1WB6; -. DR PDBsum; 2CCL; -. DR PDBsum; 2W5F; -. DR PDBsum; 2WYS; -. DR PDBsum; 2WZE; -. DR PDBsum; 3ZI7; -. DR PDBsum; 4BAG; -. DR PDBsum; 4H35; -. DR PDBsum; 5FXM; -. DR PDBsum; 6FJ4; -. DR PDBsum; 6Y8G; -. DR AlphaFoldDB; P51584; -. DR SMR; P51584; -. DR DIP; DIP-35413N; -. DR IntAct; P51584; 1. DR DrugBank; DB04522; Dexfosfoserine. DR DrugBank; DB07767; Ferulic acid. DR DrugBank; DB08711; Methyl vanillate. DR DrugBank; DB08587; Sinapic acid. DR DrugBank; DB08589; SYRINGATE. DR CAZy; CBM22; Carbohydrate-Binding Module Family 22. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR ESTHER; clotm-xyny; A85-Feruloyl-Esterase. DR BRENDA; 3.2.1.8; 1530. DR EvolutionaryTrace; P51584; -. DR GO; GO:0043263; C:cellulosome; IDA:MENGO. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW. DR CDD; cd14256; Dockerin_I; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 1.10.1330.10; Dockerin domain; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR003305; CenC_carb-bd. DR InterPro; IPR002105; Dockerin_1_rpt. DR InterPro; IPR016134; Dockerin_dom. DR InterPro; IPR036439; Dockerin_dom_sf. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR000801; Esterase-like. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR044846; GH10. DR InterPro; IPR031158; GH10_AS. DR InterPro; IPR001000; GH10_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1. DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1. DR Pfam; PF02018; CBM_4_9; 2. DR Pfam; PF00404; Dockerin_1; 1. DR Pfam; PF00756; Esterase; 1. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00633; Glyco_10; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR SUPFAM; SSF63446; Type I dockerin domain; 1. DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2. DR PROSITE; PS51766; DOCKERIN; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; KW Polysaccharide degradation; Repeat; Signal; Xylan degradation. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..1077 FT /note="Endo-1,4-beta-xylanase Y" FT /id="PRO_0000007972" FT DOMAIN 33..180 FT /note="CBM-cenC 1" FT DOMAIN 189..538 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT DOMAIN 565..714 FT /note="CBM-cenC 2" FT DOMAIN 728..796 FT /note="Dockerin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102" FT REGION 543..563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 337 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 460 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:2WYS" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:2W5F" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 107..121 FT /evidence="ECO:0007829|PDB:2W5F" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 127..138 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 143..150 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 155..166 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 170..179 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:2W5F" FT TURN 199..202 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 204..209 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 217..226 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 228..234 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 238..241 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 242..248 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:2W5F" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 260..268 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 272..279 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 286..289 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 293..297 FT /evidence="ECO:0007829|PDB:2WYS" FT HELIX 302..323 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 329..337 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 343..348 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 355..358 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 363..368 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 373..384 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 390..397 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 401..416 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 428..431 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 433..435 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 439..450 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 453..464 FT /evidence="ECO:0007829|PDB:2W5F" FT TURN 466..469 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 472..492 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 498..507 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 515..517 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 530..535 FT /evidence="ECO:0007829|PDB:2W5F" FT HELIX 541..543 FT /evidence="ECO:0007829|PDB:2W5F" FT STRAND 566..571 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 581..583 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 587..593 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 596..599 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 601..605 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 613..618 FT /evidence="ECO:0007829|PDB:1DYO" FT TURN 620..622 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 628..636 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 639..642 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 644..653 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 659..669 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 675..683 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 689..699 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 704..713 FT /evidence="ECO:0007829|PDB:1DYO" FT STRAND 738..740 FT /evidence="ECO:0007829|PDB:2CCL" FT HELIX 743..753 FT /evidence="ECO:0007829|PDB:2CCL" FT HELIX 761..767 FT /evidence="ECO:0007829|PDB:2CCL" FT HELIX 777..787 FT /evidence="ECO:0007829|PDB:2CCL" FT HELIX 817..820 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 828..836 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 839..847 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 858..863 FT /evidence="ECO:0007829|PDB:1GKL" FT TURN 876..878 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 880..889 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 896..900 FT /evidence="ECO:0007829|PDB:1GKL" FT TURN 910..912 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 913..919 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 921..928 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 934..937 FT /evidence="ECO:0007829|PDB:3ZI7" FT HELIX 938..942 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 943..947 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 948..953 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 955..967 FT /evidence="ECO:0007829|PDB:1GKL" FT TURN 968..970 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 973..978 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 983..986 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 987..1001 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 1009..1015 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 1021..1032 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 1039..1041 FT /evidence="ECO:0007829|PDB:1GKL" FT TURN 1043..1045 FT /evidence="ECO:0007829|PDB:1GKL" FT STRAND 1048..1053 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 1060..1070 FT /evidence="ECO:0007829|PDB:1GKL" FT HELIX 1071..1073 FT /evidence="ECO:0007829|PDB:1GKL" SQ SEQUENCE 1077 AA; 119673 MW; BFC8D2D22C5726A0 CRC64; MKNKRVLAKI TALVVLLGVF FVLPSNISQL YADYEVVHDT FEVNFDGWCN LGVDTYLTAV ENEGNNGTRG MMVINRSSAS DGAYSEKGFY LDGGVEYKYS VFVKHNGTGT ETFKLSVSYL DSETEEENKE VIATKDVVAG EWTEISAKYK APKTAVNITL SITTDSTVDF IFDDVTITRK GMAEANTVYA ANAVLKDMYA NYFRVGSVLN SGTVNNSSIK ALILREFNSI TCENEMKPDA TLVQSGSTNT NIRVSLNRAA SILNFCAQNN IAVRGHTLVW HSQTPQWFFK DNFQDNGNWV SQSVMDQRLE SYIKNMFAEI QRQYPSLNLY AYDVVNEAVS DDANRTRYYG GAREPGYGNG RSPWVQIYGD NKFIEKAFTY ARKYAPANCK LYYNDYNEYW DHKRDCIASI CANLYNKGLL DGVGMQSHIN ADMNGFSGIQ NYKAALQKYI NIGCDVQITE LDISTENGKF SLQQQADKYK AVFQAAVDIN RTSSKGKVTA VCVWGPNDAN TWLGSQNAPL LFNANNQPKP AYNAVASIIP QSEWGDGNNP AGGGGGGKPE EPDANGYYYH DTFEGSVGQW TARGPAEVLL SGRTAYKGSE SLLVRNRTAA WNGAQRALNP RTFVPGNTYC FSVVASFIEG ASSTTFCMKL QYVDGSGTQR YDTIDMKTVG PNQWVHLYNP QYRIPSDATD MYVYVETADD TINFYIDEAI GAVAGTVIEG PAPQPTQPPV LLGDVNGDGT INSTDLTMLK RSVLRAITLT DDAKARADVD KNGSINSTDV LLLSRYLLRV IDKFPVAENP SSSFKYESAV QYRPAPDSYL NPCPQAGRIV KETYTGINGT KSLNVYLPYG YDPNKKYNIF YLMHGGGENE NTIFSNDVKL QNILDHAIMN GELEPLIVVT PTFNGGNCTA QNFYQEFRQN VIPFVESKYS TYAESTTPQG IAASRMHRGF GGFSMGGLTT WYVMVNCLDY VAYFMPLSGD YWYGNSPQDK ANSIAEAINR SGLSKREYFV FAATGSDHIA YANMNPQIEA MKALPHFDYT SDFSKGNFYF LVAPGATHWW GYVRHYIYDA LPYFFHE //