GUND_ACET2
ID GUND_ACET2 Reviewed; 649 AA.
AC A3DDN1; P04954;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Endoglucanase D;
DE Short=EGD;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase D;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=celD; OrderedLocusNames=Cthe_0825;
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=3024110; DOI=10.1093/nar/14.21.8605;
RA Joliff G., Beguin P., Aubert J.-P.;
RT "Nucleotide sequence of the cellulase gene celD encoding endoglucanase D of
RT Clostridium thermocellum.";
RL Nucleic Acids Res. 14:8605-8613(1986).
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.
CC -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-
CC glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
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; X04584; CAA28255.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN52060.1; -; Genomic_DNA.
DR PIR; A25535; CZCLDM.
DR RefSeq; WP_011837914.1; NC_009012.1.
DR PDB; 4FL4; X-ray; 2.90 A; A/D/G/J=584-649.
DR PDBsum; 4FL4; -.
DR AlphaFoldDB; A3DDN1; -.
DR SMR; A3DDN1; -.
DR STRING; 203119.Cthe_0825; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR EnsemblBacteria; ABN52060; ABN52060; Cthe_0825.
DR KEGG; cth:Cthe_0825; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_006010_2_1_9; -.
DR OMA; KYRDGAV; -.
DR OrthoDB; 1226595at2; -.
DR BioCyc; MetaCyc:MON-16416; -.
DR EvolutionaryTrace; A3DDN1; -.
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 CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
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; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
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; Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..41
FT /evidence="ECO:0000250"
FT CHAIN 42..649
FT /note="Endoglucanase D"
FT /id="PRO_0000284722"
FT DOMAIN 579..649
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 555
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CONFLICT 577
FT /note="A -> P (in Ref. 1; CAA28255)"
FT /evidence="ECO:0000305"
FT HELIX 594..604
FT /evidence="ECO:0007829|PDB:4FL4"
FT HELIX 614..620
FT /evidence="ECO:0007829|PDB:4FL4"
FT HELIX 630..640
FT /evidence="ECO:0007829|PDB:4FL4"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:4FL4"
SQ SEQUENCE 649 AA; 72415 MW; 3A6A44735B29D3F4 CRC64;
MSRMTLKSSM KKRVLSLLIA VVFLSLTGVF PSGLIETKVS AAKITENYQF DSRIRLNSIG
FIPNHSKKAT IAANCSTFYV VKEDGTIVYT GTATSMFDND TKETVYIADF SSVNEEGTYY
LAVPGVGKSV NFKIAMNVYE DAFKTAMLGM YLLRCGTSVS ATYNGIHYSH GPCHTNDAYL
DYINGQHTKK DSTKGWHDAG DYNKYVVNAG ITVGSMFLAW EHFKDQLEPV ALEIPEKNNS
IPDFLDELKY EIDWILTMQY PDGSGRVAHK VSTRNFGGFI MPENEHDERF FVPWSSAATA
DFVAMTAMAA RIFRPYDPQY AEKCINAAKV SYEFLKNNPA NVFANQSGFS TGEYATVSDA
DDRLWAAAEM WETLGDEEYL RDFENRAAQF SKKIEADFDW DNVANLGMFT YLLSERPGKN
PALVQSIKDS LLSTADSIVR TSQNHGYGRT LGTTYYWGCN GTVVRQTMIL QVANKISPNN
DYVNAALDAI SHVFGRNYYN RSYVTGLGIN PPMNPHDRRS GADGIWEPWP GYLVGGGWPG
PKDWVDIQDS YQTNEIAINW NAALIYALAG FVNYNSAQNE VLYGDVNDDG KVNSTDLTLL
KRYVLKAVST LPSSKAEKNA DVNRDGRVNS SDVTILSRYL IRVIEKLPI
