GUNG_RUMCH
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 03-AUG-2022, entry version 148.
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; Firmicutes; 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}.
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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 EnsemblBacteria; ACL75110; ACL75110; Ccel_0731.
DR KEGG; cce:Ccel_0731; -.
DR eggNOG; COG4733; Bacteria.
DR HOGENOM; CLU_008926_0_2_9; -.
DR OMA; RWLDYWT; -.
DR OrthoDB; 1226595at2; -.
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 Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.710; -; 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 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; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF63446; SSF63446; 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
