GUN5_SALAG
ID GUN5_SALAG Reviewed; 400 AA.
AC O85465;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Endoglucanase 5A;
DE EC=3.2.1.4 {ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293};
DE AltName: Full=Alkaline cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase 5A;
DE Flags: Precursor;
GN Name=cel5A;
OS Salipaludibacillus agaradhaerens (Bacillus agaradhaerens).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=76935;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482 / PN-105;
RA Bjornvad M.E.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:1A3H, ECO:0007744|PDB:2A3H}
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 30-329 IN COMPLEX WITH
RP BETA-CELLOBIOSE, PROTEIN SEQUENCE OF 27-45, CATALYTIC ACTIVITY, AND ACTIVE
RP SITE.
RC STRAIN=ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482 / PN-105;
RX PubMed=9485319; DOI=10.1021/bi972162m;
RA Davies G.J., Dauter M., Brzozowski A.M., Bjoernvad M.E., Andersen K.V.,
RA Schuelein M.;
RT "Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6-A and
RT its cellobiose complex at 2.0-A resolution.";
RL Biochemistry 37:1926-1932(1998).
RN [3] {ECO:0007744|PDB:3A3H, ECO:0007744|PDB:4A3H, ECO:0007744|PDB:5A3H, ECO:0007744|PDB:6A3H, ECO:0007744|PDB:7A3H}
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 30-329 IN COMPLEXES WITH
RP SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RC STRAIN=ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482 / PN-105;
RX PubMed=9718293; DOI=10.1021/bi981315i;
RA Davies G.J., MacKenzie L.F., Varrot A., Dauter M., Brzozowski A.M.,
RA Schuelein M., Withers S.G.;
RT "Snapshots along an enzymatic reaction coordinate: analysis of a retaining
RT beta-glycoside hydrolase.";
RL Biochemistry 37:11707-11713(1998).
RN [4] {ECO:0007744|PDB:8A3H}
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 27-329 IN COMPLEX WITH SUBSTRATE
RP ANALOG, AND ACTIVE SITE.
RX DOI=10.1021/ja984238n;
RA Varrot A., Schulein M., Pipelier M., Vasella A., Davies G.J.;
RT "Lateral protonation of a glycosidase inhibitor. Structure of the Bacillus
RT agaradhaerens Cel5A in complex with a cellobiose-derived imidazole at 0.97
RT A resolution.";
RL J. Am. Chem. Soc. 121:2621-2622(1999).
RN [5] {ECO:0007744|PDB:1H11, ECO:0007744|PDB:1H2J, ECO:0007744|PDB:1HF6}
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 27-329 IN COMPLEXES WITH
RP SUBSTRATE ANALOGS, AND ACTIVE SITE.
RX PubMed=12595701; DOI=10.1107/s0907444902023405;
RA Varrot A., Davies G.J.;
RT "Direct experimental observation of the hydrogen-bonding network of a
RT glycosidase along its reaction coordinate revealed by atomic resolution
RT analyses of endoglucanase Cel5A.";
RL Acta Crystallogr. D 59:447-452(2003).
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 Evidence={ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9485319}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; AF067428; AAC19169.1; -; Genomic_DNA.
DR PDB; 1A3H; X-ray; 1.57 A; A=30-329.
DR PDB; 1E5J; X-ray; 1.85 A; A=27-331.
DR PDB; 1H11; X-ray; 1.08 A; A=27-329.
DR PDB; 1H2J; X-ray; 1.15 A; A=27-329.
DR PDB; 1H5V; X-ray; 1.10 A; A=27-330.
DR PDB; 1HF6; X-ray; 1.15 A; A=27-329.
DR PDB; 1OCQ; X-ray; 1.08 A; A=27-329.
DR PDB; 1QHZ; X-ray; 1.95 A; A=27-331.
DR PDB; 1QI0; X-ray; 2.10 A; A=27-331.
DR PDB; 1QI2; X-ray; 1.75 A; A=27-331.
DR PDB; 1W3K; X-ray; 1.20 A; A=27-329.
DR PDB; 1W3L; X-ray; 1.04 A; A=27-329.
DR PDB; 2A3H; X-ray; 2.00 A; A=30-329.
DR PDB; 2V38; X-ray; 1.50 A; A=27-331.
DR PDB; 3A3H; X-ray; 1.64 A; A=30-329.
DR PDB; 4A3H; X-ray; 1.65 A; A=27-329.
DR PDB; 5A3H; X-ray; 1.82 A; A=27-329.
DR PDB; 6A3H; X-ray; 1.68 A; A=27-329.
DR PDB; 7A3H; X-ray; 0.95 A; A=27-329.
DR PDB; 8A3H; X-ray; 0.97 A; A=27-329.
DR PDBsum; 1A3H; -.
DR PDBsum; 1E5J; -.
DR PDBsum; 1H11; -.
DR PDBsum; 1H2J; -.
DR PDBsum; 1H5V; -.
DR PDBsum; 1HF6; -.
DR PDBsum; 1OCQ; -.
DR PDBsum; 1QHZ; -.
DR PDBsum; 1QI0; -.
DR PDBsum; 1QI2; -.
DR PDBsum; 1W3K; -.
DR PDBsum; 1W3L; -.
DR PDBsum; 2A3H; -.
DR PDBsum; 2V38; -.
DR PDBsum; 3A3H; -.
DR PDBsum; 4A3H; -.
DR PDBsum; 5A3H; -.
DR PDBsum; 6A3H; -.
DR PDBsum; 7A3H; -.
DR PDBsum; 8A3H; -.
DR AlphaFoldDB; O85465; -.
DR SMR; O85465; -.
DR DrugBank; DB04086; 2',4'-Dinitrophenyl-2deoxy-2-Fluro-B-D-Cellobioside.
DR DrugBank; DB03584; 4-Thio-beta-D-glucopyranose.
DR DrugBank; DB04545; Afegostat.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB02061; Cellobiose.
DR DrugBank; DB01633; Deoxy-2-fluoro-beta-D-cellotrioside.
DR DrugBank; DB02017; Imidazole-Derived Cellobiose.
DR DrugBank; DB01642; methyl beta-D-glucopyranoside.
DR DrugBank; DB03862; Tetrahydrooxazine.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EvolutionaryTrace; O85465; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
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 SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; SSF51055; 1.
DR SUPFAM; SSF51445; SSF51445; 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; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:9485319"
FT CHAIN 27..400
FT /note="Endoglucanase 5A"
FT /id="PRO_0000184043"
FT DOMAIN 357..396
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000255"
FT REGION 328..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12595701,
FT ECO:0000305|PubMed:9485319, ECO:0000305|PubMed:9718293,
FT ECO:0000305|Ref.4"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1H11,
FT ECO:0007744|PDB:1QI2, ECO:0007744|PDB:5A3H,
FT ECO:0007744|PDB:6A3H, ECO:0007744|PDB:8A3H"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293,
FT ECO:0007744|PDB:1HF6, ECO:0007744|PDB:2A3H,
FT ECO:0007744|PDB:3A3H"
FT BINDING 65..66
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293,
FT ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0,
FT ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293,
FT ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0,
FT ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9718293, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:1HF6, ECO:0007744|PDB:3A3H"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6,
FT ECO:0007744|PDB:3A3H"
FT BINDING 260..261
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9718293, ECO:0007744|PDB:1HF6,
FT ECO:0007744|PDB:3A3H"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1H5V,
FT ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0,
FT ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H,
FT ECO:0007744|PDB:8A3H"
FT BINDING 293..295
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595701,
FT ECO:0000269|PubMed:9485319, ECO:0000269|PubMed:9718293,
FT ECO:0007744|PDB:1HF6, ECO:0007744|PDB:1QI0,
FT ECO:0007744|PDB:2A3H, ECO:0007744|PDB:3A3H"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:7A3H"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7A3H"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:7A3H"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:7A3H"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:1H5V"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1H5V"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:7A3H"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:7A3H"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:7A3H"
SQ SEQUENCE 400 AA; 44702 MW; 3F9C66FB9BC36FFF CRC64;
MKKITTIFVV LLMTVALFSI GNTTAADNDS VVEEHGQLSI SNGELVNERG EQVQLKGMSS
HGLQWYGQFV NYESMKWLRD DWGINVFRAA MYTSSGGYID DPSVKEKVKE AVEAAIDLDI
YVIIDWHILS DNDPNIYKEE AKDFFDEMSE LYGDYPNVIY EIANEPNGSD VTWGNQIKPY
AEEVIPIIRN NDPNNIIIVG TGTWSQDVHH AADNQLADPN VMYAFHFYAG THGQNLRDQV
DYALDQGAAI FVSEWGTSAA TGDGGVFLDE AQVWIDFMDE RNLSWANWSL THKDESSAAL
MPGANPTGGW TEAELSPSGT FVREKIRESA SIPPSDPTPP SDPGEPDPTP PSDPGEYPAW
DPNQIYTNEI VYHNGQLWQA KWWTQNQEPG DPYGPWEPLN
