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 03-MAY-2023, entry version 122. 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; Bacillota; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. 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 PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1. DR Pfam; PF03424; CBM_17_28; 1. DR Pfam; PF00150; Cellulase; 1. DR Pfam; PF00395; SLH; 3. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. 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 //