GUN7_HYPJQ
ID GUN7_HYPJQ Reviewed; 249 AA.
AC Q7Z9M7; G0RER9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 3.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Endoglucanase-7;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase-61B;
DE Short=Cel61B;
DE AltName: Full=Endo-1,4-beta-glucanase VII;
DE Short=EGVII;
DE AltName: Full=Endoglucanase VII;
DE AltName: Full=Endoglucanase-61B;
DE Flags: Precursor;
GN Name=cel61b; Synonyms=egl7; ORFNames=TRIREDRAFT_120961;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=QM6a;
RX PubMed=12788920; DOI=10.1074/jbc.m304750200;
RA Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S.,
RA Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J., Kelley A.S.,
RA Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A., Teunissen P.J.M.,
RA Yao J., Ward M.;
RT "Transcriptional regulation of biomass-degrading enzymes in the filamentous
RT fungus Trichoderma reesei.";
RL J. Biol. Chem. 278:31988-31997(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a;
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 20-249, SUBUNIT, CATALYTIC
RP ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=QM6a;
RX PubMed=18723026; DOI=10.1016/j.jmb.2008.08.016;
RA Karkehabadi S., Hansson H., Kim S., Piens K., Mitchinson C., Sandgren M.;
RT "The first structure of a glycoside hydrolase family 61 member, Cel61B from
RT Hypocrea jecorina, at 1.6 A resolution.";
RL J. Mol. Biol. 383:144-154(2008).
CC -!- FUNCTION: Has low levels of endoglucanase activity. May be involved in
CC the degradation of cellulose or lignocellulose, chitin, or other
CC polysaccharides.
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:18723026};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18723026}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18723026}.
CC -!- INDUCTION: By cellulose, lactose and sophorose.
CC {ECO:0000269|PubMed:12788920}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family. {ECO:0000305}.
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DR EMBL; AY281372; AAP57753.1; -; mRNA.
DR EMBL; GL985060; EGR50392.1; -; Genomic_DNA.
DR RefSeq; XP_006963879.1; XM_006963817.1.
DR PDB; 2VTC; X-ray; 1.60 A; A/B=1-249.
DR PDBsum; 2VTC; -.
DR AlphaFoldDB; Q7Z9M7; -.
DR SMR; Q7Z9M7; -.
DR CAZy; AA9; Auxiliary Activities 9.
DR GeneID; 18483009; -.
DR KEGG; tre:TRIREDRAFT_120961; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_120961; -.
DR eggNOG; ENOG502RY3D; Eukaryota.
DR BioCyc; MetaCyc:MON-16506; -.
DR EvolutionaryTrace; Q7Z9M7; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005103; AA9.
DR Pfam; PF03443; AA9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..249
FT /note="Endoglucanase-7"
FT /id="PRO_0000364090"
FT BINDING 20
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 195
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 78..198
FT DISULFID 120..124
FT CONFLICT 118
FT /note="V -> A (in Ref. 2; EGR50392)"
FT /evidence="ECO:0000305"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2VTC"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:2VTC"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2VTC"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2VTC"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2VTC"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2VTC"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:2VTC"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 171..182
FT /evidence="ECO:0007829|PDB:2VTC"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 193..206
FT /evidence="ECO:0007829|PDB:2VTC"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2VTC"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2VTC"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2VTC"
SQ SEQUENCE 249 AA; 26828 MW; 1BC7F179D657E0EF CRC64;
MKSCAILAAL GCLAGSVLGH GQVQNFTING QYNQGFILDY YYQKQNTGHF PNVAGWYAED
LDLGFISPDQ YTTPDIVCHK NAAPGAISAT AAAGSNIVFQ WGPGVWPHPY GPIVTYVVEC
SGSCTTVNKN NLRWVKIQEA GINYNTQVWA QQDLINQGNK WTVKIPSSLR PGNYVFRHEL
LAAHGASSAN GMQNYPQCVN IAVTGSGTKA LPAGTPATQL YKPTDPGILF NPYTTITSYT
IPGPALWQG
