ID   GUN_BACS6               Reviewed;         941 AA.
AC   P19424;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Alkaline cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
OS   Bacillus sp. (strain KSM-635).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2230718; DOI=10.1099/00221287-136-7-1327;
RA   Ozaki K., Shikata S., Kawai S., Ito S., Okamoto K.;
RT   "Molecular cloning and nucleotide sequence of a gene for alkaline cellulase
RT   from Bacillus sp. KSM-635.";
RL   J. Gen. Microbiol. 136:1327-1334(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 228-584, AND CRYSTALLIZATION.
RX   PubMed=9399567; DOI=10.1093/oxfordjournals.jbchem.a021808;
RA   Shirai T., Yamane T., Hidaka T., Kuyama K., Suzuki A., Ashida T., Ozaki K.,
RA   Ito S.;
RT   "Crystallization and preliminary X-ray analysis of a truncated family A
RT   alkaline endoglucanase isolated from Bacillus sp. KSM-635.";
RL   J. Biochem. 122:683-685(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 221-584.
RX   PubMed=11501997; DOI=10.1006/jmbi.2001.4835;
RA   Shirai T., Ishida H., Noda J., Yamane T., Ozaki K., Hakamada Y., Ito S.;
RT   "Crystal structure of alkaline cellulase K: insight into the alkaline
RT   adaptation of an industrial enzyme.";
RL   J. Mol. Biol. 310:1079-1087(2001).
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 5 (cellulase A) 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; M27420; AAA22304.1; -; Genomic_DNA.
DR   PIR; S29043; S29043.
DR   PDB; 1G01; X-ray; 1.90 A; A=228-584.
DR   PDB; 1G0C; X-ray; 1.90 A; A=228-584.
DR   PDBsum; 1G01; -.
DR   PDBsum; 1G0C; -.
DR   AlphaFoldDB; P19424; -.
DR   SMR; P19424; -.
DR   DrugBank; DB02061; Cellobiose.
DR   CAZy; CBM17; Carbohydrate-Binding Module Family 17.
DR   CAZy; CBM28; Carbohydrate-Binding Module Family 28.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EvolutionaryTrace; P19424; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005086; CBM_fam_17/28.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR001119; SLH_dom.
DR   Pfam; PF03424; CBM_17_28; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00395; SLH; 3.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR   PROSITE; PS51272; SLH; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL          1..29
FT   CHAIN           30..941
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000007838"
FT   DOMAIN          37..94
FT                   /note="SLH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   DOMAIN          95..158
FT                   /note="SLH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   DOMAIN          161..224
FT                   /note="SLH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   ACT_SITE        373
FT                   /note="Proton donor"
FT   ACT_SITE        485
FT                   /note="Nucleophile"
FT   HELIX           232..235
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:1G0C"
FT   STRAND          260..265
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           267..270
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           276..283
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          289..301
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   TURN            302..304
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           308..321
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          325..331
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           341..343
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           346..357
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          366..369
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           388..408
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          413..415
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           418..421
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           424..429
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          433..444
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   TURN            445..447
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           461..463
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           467..476
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          481..490
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   TURN            491..493
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           499..511
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          516..521
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   STRAND          524..526
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   TURN            536..538
FT                   /evidence="ECO:0007829|PDB:1G0C"
FT   HELIX           554..556
FT                   /evidence="ECO:0007829|PDB:1G01"
FT   HELIX           559..569
FT                   /evidence="ECO:0007829|PDB:1G01"
SQ   SEQUENCE   941 AA;  104628 MW;  BEA2AC3B169BFADA CRC64;
     MKIKQIKQSL SLLLIITLIM SLFVPMASAN TNESKSNAFP FSDVKKTSWS FPYIKDLYEQ
     EVITGTSATT FSPTDSVTRA QFTVMLTRGL GLEASSKDYP FKDRKNWAYK EIQAAYEAGI
     VTGKTNGEFA PNENITREQM AAMAVRAYEY LENELSLPEE QREYNDSSSI STFAQDAVQK
     AYVLELMEGN TDGYFQPKRN STREQSAKVI STLLWKVASH DYLYHTEAVK SPSEAGALQL
     VELNGQLTLA GEDGTPVQLR GMSTHGLQWF GEIVNENAFV ALSNDWGSNM IRLAMYIGEN
     GYATNPEVKD LVYEGIELAF EHDMYVIVDW HVHAPGDPRA DVYSGAYDFF EEIADHYKDH
     PKNHYIIWEL ANEPSPNNNG GPGLTNDEKG WEAVKEYAEP IVEMLREKGD NMILVGNPNW
     SQRPDLSADN PIDAENIMYS VHFYTGSHGA SHIGYPEGTP SSERSNVMAN VRYALDNGVA
     VFATEWGTSQ ANGDGGPYFD EADVWLNFLN KHNISWANWS LTNKNEISGA FTPFELGRTD
     ATDLDPGANQ VWAPEELSLS GEYVRARIKG IEYTPIDRTK FTKLVWDFND GTTQGFQVNG
     DSPNKESITL SNNNDALQIE GLNVSNDISE GNYWDNVRLS ADGWSENVDI LGATELTIDV
     IVEEPTTVSI AAIPQGPAAG WANPTRAIKV TEDDFESFGD GYKALVTITS EDSPSLETIA
     TSPEDNTMSN IILFVGTEDA DVISLDNITV SGTEIEIEVI HDEKGTATLP STFEDGTRQG
     WDWHTESGVK TALTIEEANG SNALSWEYAY PEVKPSDGWA TAPRLDFWKD ELVRGTSDYI
     SFDFYIDAVR ASEGAISINA VFQPPANGYW QEVPTTFEID LTELDSATVT SDELYHYEVK
     INIRDIEAIT DDTELRNLLL IFADEDSDFA GRVFVDNVRF E