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Database: UniProt
Entry: W7QGK5_9ALTE
LinkDB: W7QGK5_9ALTE
Original site: W7QGK5_9ALTE 
ID   W7QGK5_9ALTE            Unreviewed;       588 AA.
AC   W7QGK5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=DS2_05715 {ECO:0000313|EMBL:EWH11041.1};
OS   Catenovulum agarivorans DS-2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Catenovulum.
OX   NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH11041.1, ECO:0000313|Proteomes:UP000019276};
RN   [1] {ECO:0000313|EMBL:EWH11041.1, ECO:0000313|Proteomes:UP000019276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-2 {ECO:0000313|EMBL:EWH11041.1,
RC   ECO:0000313|Proteomes:UP000019276};
RX   PubMed=24604650;
RA   Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT   "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT   Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL   Genome Announc. 2:e00144-14(2014).
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:0000256|RuleBase:RU361166};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU10059, ECO:0000256|RuleBase:RU361166}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWH11041.1}.
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DR   EMBL; ARZY01000007; EWH11041.1; -; Genomic_DNA.
DR   RefSeq; WP_035013713.1; NZ_ARZY01000007.1.
DR   AlphaFoldDB; W7QGK5; -.
DR   STRING; 1328313.DS2_05715; -.
DR   PATRIC; fig|1328313.3.peg.1178; -.
DR   eggNOG; COG3291; Bacteria.
DR   OrthoDB; 9808897at2; -.
DR   Proteomes; UP000019276; Unassembled WGS sequence.
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; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
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   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019276}.
FT   DOMAIN          48..125
FT                   /note="Cellulase Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF02927"
FT   DOMAIN          137..580
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        517
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        559
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        568
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   588 AA;  65002 MW;  5C88DD33DFEDDC05 CRC64;
     MKKQLFSGCA IGLSAVLLIG CQGTDNIASE SSIQAPSKPK QQPADEVAAV LYNQIGYQAN
     MAKLIYLQAN NALTVDVVDR NNQQSVISKL TSEAQFWPHA GKNFVELDLT ELSQVGEYQI
     VIDGEVLASF RVANDVYTRA TKIIAQGFYF NRASHEISFE YGGKFNRAAG HMDQQVKIHH
     SAASAHRPEG TVVPSPKGWY DAGDYNKYTV NSAISMYTML RAYLKHPSFF QQLKLNIPEQ
     FNSTADILDE LFWQLDWFLT MQDPNDGGVY HKVTTLNFSG KIMPEAGLEP RYMIAKSIGA
     SLDFAATTAY FARHLQDIDA ERAKLCAQAA EQAYKWAKAN PDKIYVQPDD VKTGAYVVTG
     DDYSDEWFWA AAELALTFDA KDYWQDLTQL QAIEMSVPTW SDVQGLGWIS LAEEANAQQW
     QYKAQQKLKA LAEHMSIMAN QSAIKVSLGV FDDDFVWGSN GNMANHIMVL DAAKAYVADP
     ASLNRLIATN LDYIFGTNPT GYSFVSGLGS QTPMHLHHRV SEADDVLDPV PGLVAGGPHA
     GQQDQCDYPS KFPALSYVDD WCSYATNETA INWNAPLLYA VASVASEE
//
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