ID XYNZ_ACET2 Reviewed; 837 AA. AC P10478; A3DGV2; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 3. DT 27-MAR-2024, entry version 165. DE RecName: Full=Endo-1,4-beta-xylanase Z; DE Short=Xylanase Z; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase Z; DE Flags: Precursor; GN Name=xynZ; OrderedLocusNames=Cthe_1963; OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=203119; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3139632; DOI=10.1128/jb.170.10.4582-4588.1988; RA Grepinet O., Chebrou M.-C., Beguin P.; RT "Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of RT Clostridium thermocellum."; RL J. Bacteriol. 170:4582-4588(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., RA Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 515-837. RX PubMed=7664125; DOI=10.1038/nsb0795-569; RA Dominguez R., Souchon H., Spinelli S., Dauter Z., Wilson K.S., Chauvaux S., RA Beguin P., Alzari P.M.; RT "A common protein fold and similar active site in two distinct families of RT beta-glycanases."; RL Nat. Struct. Biol. 2:569-576(1995). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; 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; M22624; AAA23286.1; -; Genomic_DNA. DR EMBL; CP000568; ABN53181.1; -; Genomic_DNA. DR PIR; A31842; A31842. DR RefSeq; WP_003513959.1; NC_009012.1. DR PDB; 1JJF; X-ray; 1.75 A; A=20-287. DR PDB; 1JT2; X-ray; 1.80 A; A=20-287. DR PDB; 1XYZ; X-ray; 1.40 A; A/B=491-837. DR PDBsum; 1JJF; -. DR PDBsum; 1JT2; -. DR PDBsum; 1XYZ; -. DR AlphaFoldDB; P10478; -. DR SMR; P10478; -. DR IntAct; P10478; 1. DR STRING; 203119.Cthe_1963; -. DR DrugBank; DB07767; Ferulic acid. DR CAZy; CBM6; Carbohydrate-Binding Module Family 6. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR ESTHER; clotm-xynz; A85-Feruloyl-Esterase. DR KEGG; cth:Cthe_1963; -. DR eggNOG; COG2382; Bacteria. DR eggNOG; COG3507; Bacteria. DR eggNOG; COG3693; Bacteria. DR HOGENOM; CLU_339412_0_0_9; -. DR OrthoDB; 9777383at2; -. DR BioCyc; MetaCyc:MONOMER-16453; -. DR BRENDA; 3.1.1.73; 1530. DR BRENDA; 3.2.1.73; 1530. DR BRENDA; 3.2.1.8; 1530. DR EvolutionaryTrace; P10478; -. DR Proteomes; UP000002145; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:MENGO. DR GO; GO:0033905; F:xylan endo-1,3-beta-xylosidase activity; IDA:MENGO. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW. DR CDD; cd04084; CBM6_xylanase-like; 1. 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; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR006584; Cellulose-bd_IV. DR InterPro; IPR005084; CMB_fam6. 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; PF03422; CBM_6; 1. DR Pfam; PF00404; Dockerin_1; 1. DR Pfam; PF00756; Esterase; 1. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00606; CBD_IV; 1. 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; 1. DR SUPFAM; SSF63446; Type I dockerin domain; 1. DR PROSITE; PS51175; CBM6; 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; Disulfide bond; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Signal; KW Xylan degradation. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..837 FT /note="Endo-1,4-beta-xylanase Z" FT /id="PRO_0000007973" FT DOMAIN 299..420 FT /note="CBM6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523" FT DOMAIN 424..492 FT /note="Dockerin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102" FT DOMAIN 512..833 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT ACT_SITE 645 FT /note="Proton donor" FT ACT_SITE 754 FT /note="Nucleophile" FT DISULFID 783..789 FT /evidence="ECO:0000250" FT TURN 37..40 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 50..58 FT /evidence="ECO:0007829|PDB:1JJF" FT TURN 59..62 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 63..71 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:1JJF" FT TURN 94..102 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 104..113 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 137..147 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 149..156 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 166..171 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 173..183 FT /evidence="ECO:0007829|PDB:1JJF" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 204..207 FT /evidence="ECO:0007829|PDB:1JJF" FT TURN 209..212 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 220..227 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 233..245 FT /evidence="ECO:0007829|PDB:1JJF" FT STRAND 251..255 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 262..279 FT /evidence="ECO:0007829|PDB:1JJF" FT TURN 280..282 FT /evidence="ECO:0007829|PDB:1JJF" FT HELIX 518..524 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 528..533 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 536..539 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 543..552 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 554..560 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 564..567 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 577..588 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 592..599 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 601..603 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 606..609 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 615..632 FT /evidence="ECO:0007829|PDB:1XYZ" FT TURN 633..636 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 638..645 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 651..654 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 658..663 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 667..678 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 682..690 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 692..695 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 696..710 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 717..720 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 723..727 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 730..745 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 749..760 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 765..785 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 789..795 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 804..807 FT /evidence="ECO:0007829|PDB:1XYZ" FT STRAND 815..817 FT /evidence="ECO:0007829|PDB:1XYZ" FT HELIX 825..834 FT /evidence="ECO:0007829|PDB:1XYZ" SQ SEQUENCE 837 AA; 92263 MW; DD4C29F04D12B6CD CRC64; MSRKLFSVLL VGLMLMTSLL VTISSTSAAS LPTMPPSGYD QVRNGVPRGQ VVNISYFSTA TNSTRPARVY LPPGYSKDKK YSVLYLLHGI GGSENDWFEG GGRANVIADN LIAEGKIKPL IIVTPNTNAA GPGIADGYEN FTKDLLNSLI PYIESNYSVY TDREHRAIAG LSMGGGQSFN IGLTNLDKFA YIGPISAAPN TYPNERLFPD GGKAAREKLK LLFIACGTND SLIGFGQRVH EYCVANNINH VYWLIQGGGH DFNVWKPGLW NFLQMADEAG LTRDGNTPVP TPSPKPANTR IEAEDYDGIN SSSIEIIGVP PEGGRGIGYI TSGDYLVYKS IDFGNGATSF KAKVANANTS NIELRLNGPN GTLIGTLSVK STGDWNTYEE QTCSISKVTG INDLYLVFKG PVNIDWFTFG VESSSTGLGD LNGDGNINSS DLQALKRHLL GISPLTGEAL LRADVNRSGK VDSTDYSVLK RYILRIITEF PGQGDVQTPN PSVTPTQTPI PTISGNALRD YAEARGIKIG TCVNYPFYNN SDPTYNSILQ REFSMVVCEN EMKFDALQPR QNVFDFSKGD QLLAFAERNG MQMRGHTLIW HNQNPSWLTN GNWNRDSLLA VMKNHITTVM THYKGKIVEW DVANECMDDS GNGLRSSIWR NVIGQDYLDY AFRYAREADP DALLFYNDYN IEDLGPKSNA VFNMIKSMKE RGVPIDGVGF QCHFINGMSP EYLASIDQNI KRYAEIGVIV SFTEIDIRIP QSENPATAFQ VQANNYKELM KICLANPNCN TFVMWGFTDK YTWIPGTFPG YGNPLIYDSN YNPKPAYNAI KEALMGY //