GUNA_RUMCH
ID GUNA_RUMCH Reviewed; 475 AA.
AC P17901; B8HZV8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Endoglucanase A;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase A;
DE AltName: Full=EGCCA;
DE AltName: Full=Endo-1,4-beta-glucanase A;
DE Flags: Precursor;
GN Name=celCCA; OrderedLocusNames=Ccel_1099;
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], AND PROTEIN SEQUENCE OF 27-39.
RX PubMed=2558058; DOI=10.1016/0378-1119(89)90137-6;
RA Faure E., Belaich A., Bagnara C., Gaudin C., Belaich J.-P.;
RT "Sequence analysis of the Clostridium cellulolyticum endoglucanase-A-
RT encoding gene, celCCA.";
RL Gene 84:39-46(1989).
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.
RN [3]
RP CHARACTERIZATION.
RX PubMed=1744052; DOI=10.1128/jb.173.24.7956-7962.1991;
RA Fierobe H.-P., Gaudin C., Belaich A., Loufti M., Faure E., Bagnara C.,
RA Baty D., Belaich J.-P.;
RT "Characterization of endoglucanase A from Clostridium cellulolyticum.";
RL J. Bacteriol. 173:7956-7962(1991).
RN [4]
RP MUTAGENESIS OF ARG-104; HIS-147 AND HIS-148.
RX PubMed=1624455; DOI=10.1128/jb.174.14.4677-4682.1992;
RA Belaich A., Fierobe H.-P., Baty D., Busetta B., Bagnara-Tardif C.,
RA Gaudin C., Belaich J.-P.;
RT "The catalytic domain of endoglucanase A from Clostridium cellulolyticum:
RT effects of arginine 79 and histidine 122 mutations on catalysis.";
RL J. Bacteriol. 174:4677-4682(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 27-406.
RX PubMed=8535787; DOI=10.1016/s0969-2126(01)00228-3;
RA Ducros V., Czjzek M., Belaich A., Gaudin C., Fierobe H.P., Belaich J.-P.,
RA Davies G.J., Haser R.;
RT "Crystal structure of the catalytic domain of a bacterial cellulase
RT belonging to family 5.";
RL Structure 3:939-949(1995).
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 -!- MISCELLANEOUS: The C-terminus (AA 411-475) may play a role in
CC organizing the cellulosome complex.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; M93096; AAA51444.1; -; Genomic_DNA.
DR EMBL; M32362; AAA23221.1; -; Genomic_DNA.
DR EMBL; CP001348; ACL75458.1; -; Genomic_DNA.
DR RefSeq; WP_015924614.1; NC_011898.1.
DR PDB; 1EDG; X-ray; 1.60 A; A=27-401.
DR PDB; 2VN5; X-ray; 1.90 A; B/D=410-475.
DR PDB; 2VN6; X-ray; 1.49 A; B=410-472.
DR PDBsum; 1EDG; -.
DR PDBsum; 2VN5; -.
DR PDBsum; 2VN6; -.
DR AlphaFoldDB; P17901; -.
DR SMR; P17901; -.
DR STRING; 394503.Ccel_1099; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblBacteria; ACL75458; ACL75458; Ccel_1099.
DR KEGG; cce:Ccel_1099; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_018668_3_1_9; -.
DR OMA; YVILNTH; -.
DR OrthoDB; 1395441at2; -.
DR EvolutionaryTrace; P17901; -.
DR Proteomes; UP000001349; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1330.10; -; 1.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2558058"
FT CHAIN 27..475
FT /note="Endoglucanase A"
FT /id="PRO_0000007845"
FT DOMAIN 409..474
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT ACT_SITE 147
FT /evidence="ECO:0000305"
FT ACT_SITE 195
FT /note="Proton donor"
FT ACT_SITE 332
FT /note="Nucleophile"
FT MUTAGEN 104
FT /note="R->K: Small loss of activity."
FT /evidence="ECO:0000269|PubMed:1624455"
FT MUTAGEN 104
FT /note="R->S,V: Large decrease of activity."
FT /evidence="ECO:0000269|PubMed:1624455"
FT MUTAGEN 147
FT /note="H->S,E,G,F: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:1624455"
FT MUTAGEN 148
FT /note="H->V: Large decrease of activity."
FT /evidence="ECO:0000269|PubMed:1624455"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1EDG"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:1EDG"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1EDG"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:1EDG"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1EDG"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 212..234
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:1EDG"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1EDG"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:1EDG"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:2VN6"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:2VN6"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:2VN6"
FT HELIX 455..465
FT /evidence="ECO:0007829|PDB:2VN6"
SQ SEQUENCE 475 AA; 53625 MW; 1AF20EA2C0A132F9 CRC64;
MKKTTAFLLC FLMIFTALLP MQNANAYDAS LIPNLQIPQK NIPNNDGMNF VKGLRLGWNL
GNTFDAFNGT NITNELDYET SWSGIKTTKQ MIDAIKQKGF NTVRIPVSWH PHVSGSDYKI
SDVWMNRVQE VVNYCIDNKM YVILNTHHDV DKVKGYFPSS QYMASSKKYI TSVWAQIAAR
FANYDEHLIF EGMNEPRLVG HANEWWPELT NSDVVDSINC INQLNQDFVN TVRATGGKNA
SRYLMCPGYV ASPDGATNDY FRMPNDISGN NNKIIVSVHA YCPWNFAGLA MADGGTNAWN
INDSKDQSEV TWFMDNIYNK YTSRGIPVII GECGAVDKNN LKTRVEYMSY YVAQAKARGI
LCILWDNNNF SGTGELFGFF DRRSCQFKFP EIIDGMVKYA FEAKTDPDPV IVYGDYNNDG
NVDALDFAGL KKYIMAADHA YVKNLDVNLD NEVNAFDLAI LKKYLLGMVS KLPSN
