XYNZ_ACET2
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 03-AUG-2022, entry version 158.
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; Firmicutes; 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 / NRRL
RC 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 PRIDE; P10478; -.
DR EnsemblBacteria; ABN53181; ABN53181; Cthe_1963.
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 OMA; HEYCVAN; -.
DR OrthoDB; 654705at2; -.
DR BioCyc; MetaCyc:MON-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 Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 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; PTHR31490; 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; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF63446; SSF63446; 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
