ID   GUNZ_THEST              Reviewed;         986 AA.
AC   P23659;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-MAY-2023, entry version 111.
DE   RecName: Full=Endoglucanase Z;
DE            EC=3.2.1.4;
DE   AltName: Full=Avicelase I;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Thermoactive cellulase;
DE   Flags: Precursor;
GN   Name=celZ;
OS   Thermoclostridium stercorarium (Clostridium stercorarium).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Thermoclostridium.
OX   NCBI_TaxID=1510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-36 AND
RP   475-486.
RC   STRAIN=NCIB 11745;
RX   PubMed=2250652; DOI=10.1007/bf00265062;
RA   Jauris S., Ruecknagel K.P., Schwarz W.H., Kratzsch P., Bronnenmeier K.,
RA   Staudenbauer W.L.;
RT   "Sequence analysis of the Clostridium stercorarium celZ gene encoding a
RT   thermoactive cellulase (Avicelase I): identification of catalytic and
RT   cellulose-binding domains.";
RL   Mol. Gen. Genet. 223:258-267(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR   EMBL; X55299; CAA39010.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S12021; S12021.
DR   AlphaFoldDB; P23659; -.
DR   SMR; P23659; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR005102; Carbo-bd_X2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF00942; CBM_3; 2.
DR   Pfam; PF03442; CBM_X2; 2.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM01067; CBM_3; 2.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR   SUPFAM; SSF81296; E set domains; 2.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51172; CBM3; 2.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:2250652"
FT   CHAIN           26..986
FT                   /note="Endoglucanase Z"
FT                   /id="PRO_0000007948"
FT   DOMAIN          481..642
FT                   /note="CBM3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   REPEAT          651..738
FT                   /note="Domain B"
FT   REPEAT          744..831
FT                   /note="Domain B'"
FT   DOMAIN          836..986
FT                   /note="CBM3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   ACT_SITE        84
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        447
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   986 AA;  109512 MW;  1802E09B22923690 CRC64;
     MRKFYSFAII ISLLVTGLFI HTPKAEAAGY NYGEALQKAI MFYEFQRSGK LPENKRDNWR
     GDSGLNDGAD VGLDLTGGWY DAGDHVKFNL PMAYSQTMLA WAAYEAEEAL ERSGQMGYLL
     DAIKWVSDYL IKCHPSPNVF YYQVGDGHLD HSWWGPAEVM QMDRPAYKVD LANPGSTVVA
     EAAAALASAA VVFADRDPAY AATCIQHAKE LYNFAEITKS DSGYTAASGF YDSHSGFYDE
     LSWAGVWLYL ATGDETYLNK AEQYVAYWGT EPQTNIISYK WAHCWDDVHY GACLLLAKIT
     GKQIYKEAIE RHLDYWSVGY NGERVHYTPK GLAWLDSWGS LRYATTTAFL ASVYADWEGC
     SREKAAIYND FAKQQIDYAL GSSGRSYVVG FGVNPPKRPH HRTAHSSWAD SMSVPDYHRH
     VLIGALVGGP GKDDSYTDDI NNYINNEVAC DYNAGFVGAL AKMYEDYGGS PIPDLNAFEE
     ITNDEFFVMA GINASGQNFI EIKALLHNQS GWPARVADKL SFRYFVDLTE LIEAGYSASD
     VTITTNYNAG AKVTGLHPWN EAENIYYVNV DFTGTKIYPG GQSAYRKEVQ FRIAAPQNTN
     FWNNDNDYSF RDIKGVTSGN TVKTVYIPVY DDGVLVFGVE PEGGSGENNS SISITNATFD
     KNPAKQENIQ VVMNLNGNTL NGIKYGNTYL REGTDYTVSG DTVTILKSFL NSFDTSTVQL
     IFDFSAGRDP VLTVNIIDTT TSASIVPTTA DFDKNPDASR DVKVKLVPNG NTLLAVKKDG
     EALVLGRDYS IDGDEVTIFR EYLADQPVGR VTLTFDFDRG TDPVLTINIT DSRQVETGVI
     QIQMFNGNTS DKTNGIMPRY RLTNTGTTPI RLSDVKIRYY YTIDGEKDQN FWCDWSSVGS
     NNITGTFVKM AEPKEGADYY LETGFTDGAG YLQPNQSIEV QNRFSKADWT DYIQTNDYSF
     STNTSYGSND RITVYISGVL VSGIEP
//