ID GUNG_RUMCH Reviewed; 725 AA. AC P37700; B8I7V3; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 2. DT 27-MAR-2024, entry version 153. DE RecName: Full=Endoglucanase G; DE EC=3.2.1.4; DE AltName: Full=Cellulase G; DE AltName: Full=EGCCG; DE AltName: Full=Endo-1,4-beta-glucanase G; DE Flags: Precursor; GN Name=celCCG; OrderedLocusNames=Ccel_0731; OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / OS H10) (Clostridium cellulolyticum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminiclostridium. OX NCBI_TaxID=394503; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1398087; DOI=10.1016/0378-1119(92)90062-t; RA Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., RA Belaich J.-P.; RT "Sequence analysis of a gene cluster encoding cellulases from Clostridium RT cellulolyticum."; RL Gene 119:17-28(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Zhou J., Richardson P.; RT "Complete sequence of Clostridium cellulolyticum H10."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The biological conversion of cellulose to glucose generally CC requires three types of hydrolytic enzymes: (1) Endoglucanases which CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that CC cut the disaccharide cellobiose from the non-reducing end of the CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the CC cellobiose and other short cello-oligosaccharides to glucose. 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 -!- PATHWAY: Glycan metabolism; cellulose degradation. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family. CC {ECO:0000255|PROSITE-ProRule:PRU10140, 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; M87018; AAA73868.1; -; Genomic_DNA. DR EMBL; CP001348; ACL75110.1; -; Genomic_DNA. DR PIR; JC1300; JC1300. DR RefSeq; WP_015924277.1; NC_011898.1. DR PDB; 1G87; X-ray; 1.60 A; A/B=36-649. DR PDB; 1GA2; X-ray; 1.70 A; A/B=36-649. DR PDB; 1K72; X-ray; 1.80 A; A/B=36-649. DR PDB; 1KFG; X-ray; 1.90 A; A/B=36-649. DR PDBsum; 1G87; -. DR PDBsum; 1GA2; -. DR PDBsum; 1K72; -. DR PDBsum; 1KFG; -. DR AlphaFoldDB; P37700; -. DR SMR; P37700; -. DR STRING; 394503.Ccel_0731; -. DR DrugBank; DB03859; 1-thio-beta-D-glucopyranose. DR DrugBank; DB03584; 4-Thio-beta-D-glucopyranose. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB02061; Cellobiose. DR DrugBank; DB02361; S-Methyl Thiocysteine Group. DR CAZy; CBM3; Carbohydrate-Binding Module Family 3. DR CAZy; GH9; Glycoside Hydrolase Family 9. DR KEGG; cce:Ccel_0731; -. DR eggNOG; COG4733; Bacteria. DR HOGENOM; CLU_008926_0_2_9; -. DR OrthoDB; 9758662at2; -. DR UniPathway; UPA00696; -. DR EvolutionaryTrace; P37700; -. DR Proteomes; UP000001349; Chromosome. 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-UniPathway. DR CDD; cd14256; Dockerin_I; 1. DR Gene3D; 1.50.10.10; -; 1. DR Gene3D; 1.10.1330.10; Dockerin domain; 1. DR Gene3D; 2.60.40.710; Endoglucanase-like; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR001956; CBM3. DR InterPro; IPR036966; CBM3_sf. DR InterPro; IPR002105; Dockerin_1_rpt. DR InterPro; IPR016134; Dockerin_dom. DR InterPro; IPR036439; Dockerin_dom_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 PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1. DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1. DR Pfam; PF00942; CBM_3; 1. DR Pfam; PF00404; Dockerin_1; 1. DR Pfam; PF00759; Glyco_hydro_9; 1. DR SMART; SM01067; CBM_3; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. DR SUPFAM; SSF63446; Type I dockerin domain; 1. DR PROSITE; PS51172; CBM3; 1. DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1. DR PROSITE; PS51766; DOCKERIN; 1. DR PROSITE; PS00018; EF_HAND_1; 1. 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 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Signal. FT SIGNAL 1..35 FT /evidence="ECO:0000255" FT CHAIN 36..725 FT /note="Endoglucanase G" FT /id="PRO_0000007947" FT DOMAIN 489..650 FT /note="CBM3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513" FT DOMAIN 658..724 FT /note="Dockerin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102" FT ACT_SITE 93 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140" FT ACT_SITE 408 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059" FT ACT_SITE 446 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060" FT ACT_SITE 455 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060" FT CONFLICT 609..610 FT /note="TT -> RR (in Ref. 1; AAA73868)" FT /evidence="ECO:0000305" FT HELIX 41..55 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:1G87" FT TURN 74..77 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 98..122 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 125..141 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 149..154 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 185..202 FT /evidence="ECO:0007829|PDB:1G87" FT TURN 203..205 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 207..227 FT /evidence="ECO:0007829|PDB:1G87" FT TURN 235..239 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 246..260 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 263..271 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 272..275 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 282..285 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 297..308 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 311..324 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 348..364 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 373..388 FT /evidence="ECO:0007829|PDB:1G87" FT TURN 389..391 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 399..402 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 410..413 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 416..418 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 451..454 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 458..475 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 493..504 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 507..516 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 527..535 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 537..541 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 546..548 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 549..552 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 556..558 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 567..570 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 571..573 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 575..581 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 589..591 FT /evidence="ECO:0007829|PDB:1G87" FT TURN 592..595 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 596..604 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 614..616 FT /evidence="ECO:0007829|PDB:1G87" FT HELIX 618..620 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 625..628 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 633..635 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 637..639 FT /evidence="ECO:0007829|PDB:1G87" FT STRAND 642..646 FT /evidence="ECO:0007829|PDB:1G87" SQ SEQUENCE 725 AA; 79776 MW; 1C87FE4D03797C41 CRC64; MLKTKRKLTK AIGVALSISI LSSLVSFIPQ TNTYAAGTYN YGEALQKSIM FYEFQRSGDL PADKRDNWRD DSGMKDGSDV GVDLTGGWYD AGDHVKFNLP MSYTSAMLAW SLYEDKDAYD KSGQTKYIMD GIKWANDYFI KCNPTPGVYY YQVGDGGKDH SWWGPAEVMQ MERPSFKVDA SKPGSAVCAS TAASLASAAV VFKSSDPTYA EKCISHAKNL FDMADKAKSD AGYTAASGYY SSSSFYDDLS WAAVWLYLAT NDSTYLDKAE SYVPNWGKEQ QTDIIAYKWG QCWDDVHYGA ELLLAKLTNK QLYKDSIEMN LDFWTTGVNG TRVSYTPKGL AWLFQWGSLR HATTQAFLAG VYAEWEGCTP SKVSVYKDFL KSQIDYALGS TGRSFVVGYG VNPPQHPHHR TAHGSWTDQM TSPTYHRHTI YGALVGGPDN ADGYTDEINN YVNNEIACDY NAGFTGALAK MYKHSGGDPI PNFKAIEKIT NDEVIIKAGL NSTGPNYTEI KAVVYNQTGW PARVTDKISF KYFMDLSEIV AAGIDPLSLV TSSNYSEGKN TKVSGVLPWD VSNNVYYVNV DLTGENIYPG GQSACRREVQ FRIAAPQGTT YWNPKNDFSY DGLPTTSTVN TVTNIPVYDN GVKVFGNEPA GGSENPDPEI LYGDVNSDKN VDALDFAALK KYLLGGTSSI DVKAADTYKD GNIDAIDMAT LKKYLLGTIT QLPQG //