GUNA_ACET2
ID GUNA_ACET2 Reviewed; 477 AA.
AC A3DC29; P04955;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Endoglucanase A;
DE Short=EGA;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase A;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=celA; OrderedLocusNames=Cthe_0269;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3980433; DOI=10.1128/jb.162.1.102-105.1985;
RA Beguin P., Cornet P., Aubert J.-P.;
RT "Sequence of a cellulase gene of the thermophilic bacterium Clostridium
RT thermocellum.";
RL J. Bacteriol. 162:102-105(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 33-395.
RX PubMed=8805535; DOI=10.1016/s0969-2126(96)00031-7;
RA Alzari P.M., Souchon H., Dominguez R.;
RT "The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase
RT from Clostridium thermocellum.";
RL Structure 4:265-275(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF 33-395.
RX PubMed=12198299; DOI=10.1107/s0907444902011368;
RA Schmidt A., Gonzalez A., Morris R.J., Costabel M., Alzari P.M.,
RA Lamzin V.S.;
RT "Advantages of high-resolution phasing: MAD to atomic resolution.";
RL Acta Crystallogr. D 58:1433-1441(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS) OF 33-395.
RX PubMed=11884144; DOI=10.1006/jmbi.2001.5404;
RA Guerin D.M., Lascombe M.B., Costabel M., Souchon H., Lamzin V., Beguin P.,
RA Alzari P.M.;
RT "Atomic (0.94 A) resolution structure of an inverting glycosidase in
RT complex with substrate.";
RL J. Mol. Biol. 316:1061-1069(2002).
CC -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-
CC glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
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 8 (cellulase D) family.
CC {ECO:0000305}.
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DR EMBL; K03088; AAA83521.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN51508.1; -; Genomic_DNA.
DR PIR; A23100; CZCLAM.
DR RefSeq; WP_003512420.1; NC_009012.1.
DR PDB; 1CEM; X-ray; 1.65 A; A=33-395.
DR PDB; 1IS9; X-ray; 1.03 A; A=33-395.
DR PDB; 1KWF; X-ray; 0.94 A; A=33-395.
DR PDBsum; 1CEM; -.
DR PDBsum; 1IS9; -.
DR PDBsum; 1KWF; -.
DR AlphaFoldDB; A3DC29; -.
DR SMR; A3DC29; -.
DR STRING; 203119.Cthe_0269; -.
DR CAZy; GH8; Glycoside Hydrolase Family 8.
DR EnsemblBacteria; ABN51508; ABN51508; Cthe_0269.
DR KEGG; cth:Cthe_0269; -.
DR eggNOG; COG3405; Bacteria.
DR HOGENOM; CLU_036185_0_0_9; -.
DR OMA; CRTPWRL; -.
DR OrthoDB; 636673at2; -.
DR BioCyc; MetaCyc:MON-16413; -.
DR BRENDA; 3.2.1.4; 1530.
DR EvolutionaryTrace; A3DC29; -.
DR Proteomes; UP000002145; 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 Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
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; IPR002037; Glyco_hydro_8.
DR InterPro; IPR019834; Glyco_hydro_8_CS.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF01270; Glyco_hydro_8; 1.
DR PRINTS; PR00735; GLHYDRLASE8.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 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..32
FT /evidence="ECO:0000250"
FT CHAIN 33..477
FT /note="Endoglucanase A"
FT /id="PRO_0000284721"
FT DOMAIN 411..477
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT ACT_SITE 95
FT /note="Proton donor"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1KWF"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 52..70
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:1KWF"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1KWF"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1KWF"
FT TURN 142..147
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:1KWF"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:1KWF"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1KWF"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:1KWF"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1KWF"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1KWF"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:1KWF"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1KWF"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:1KWF"
SQ SEQUENCE 477 AA; 52594 MW; BA5A0AD5022E8A51 CRC64;
MKNVKKRVGV VLLILAVLGV YMLAMPANTV SAAGVPFNTK YPYGPTSIAD NQSEVTAMLK
AEWEDWKSKR ITSNGAGGYK RVQRDASTNY DTVSEGMGYG LLLAVCFNEQ ALFDDLYRYV
KSHFNGNGLM HWHIDANNNV TSHDGGDGAA TDADEDIALA LIFADKLWGS SGAINYGQEA
RTLINNLYNH CVEHGSYVLK PGDRWGGSSV TNPSYFAPAW YKVYAQYTGD TRWNQVADKC
YQIVEEVKKY NNGTGLVPDW CTASGTPASG QSYDYKYDAT RYGWRTAVDY SWFGDQRAKA
NCDMLTKFFA RDGAKGIVDG YTIQGSKISN NHNASFIGPV AAASMTGYDL NFAKELYRET
VAVKDSEYYG YYGNSLRLLT LLYITGNFPN PLSDLSGQPT PPSNPTPSLP PQVVYGDVNG
DGNVNSTDLT MLKRYLLKSV TNINREAADV NRDGAINSSD MTILKRYLIK SIPHLPY
