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Database: UniProt
Entry: P10476
LinkDB: P10476
Original site: P10476 
ID   GUNA_CELJU              Reviewed;         962 AA.
AC   P10476; B3PKK4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-SEP-2014, entry version 109.
DE   RecName: Full=Endoglucanase A;
DE            Short=EGA;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=celA; Synonyms=cel9A; OrderedLocusNames=CJA_2472;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2851699; DOI=10.1007/BF00333406;
RA   Hall J., Gilbert H.J.;
RT   "The nucleotide sequence of a carboxymethylcellulase gene from
RT   Pseudomonas fluorescens subsp. cellulosa.";
RL   Mol. Gen. Genet. 213:112-117(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of
RT   the soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM10 (carbohydrate binding type-10)
CC       domain.
CC   -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
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DR   EMBL; X12570; CAA31082.1; -; Genomic_DNA.
DR   EMBL; CP000934; ACE85757.1; -; Genomic_DNA.
DR   RefSeq; WP_012488069.1; NC_010995.1.
DR   RefSeq; YP_001982933.1; NC_010995.1.
DR   ProteinModelPortal; P10476; -.
DR   STRING; 498211.CJA_2472; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   EnsemblBacteria; ACE85757; ACE85757; CJA_2472.
DR   GeneID; 6416717; -.
DR   KEGG; cja:CJA_2472; -.
DR   PATRIC; 21328310; VBICelJap122165_2424.
DR   HOGENOM; HOG000245359; -.
DR   OrthoDB; EOG6QRW4D; -.
DR   BioCyc; CJAP498211:GHIT-2463-MONOMER; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.30.32.30; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR012341; 6hp_glycosidase.
DR   InterPro; IPR008965; Carb-bd_dom.
DR   InterPro; IPR012291; CBD_carb-bd_dom.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR009031; CBM_fam10.
DR   InterPro; IPR001919; Cellulose-bd_dom_fam2_bac.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR018221; Glyco_hydro_9_AS.
DR   InterPro; IPR004197; Glyco_hydro_9_Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR000601; PKD_dom.
DR   Pfam; PF02013; CBM_10; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   Pfam; PF00801; PKD; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM01064; CBM_10; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49299; SSF49299; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF57615; SSF57615; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1; 1.
DR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Complete proteome;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Signal.
FT   SIGNAL        1     32       Potential.
FT   CHAIN        33    962       Endoglucanase A.
FT                                /FTId=PRO_0000007957.
FT   DOMAIN      671    697       CBM10.
FT   DOMAIN      859    962       CBM2.
FT   COMPBIAS    608    664       Ser-rich.
FT   COMPBIAS    823    859       Ser-rich (linker).
FT   ACT_SITE    523    523       By similarity.
FT   ACT_SITE    573    573       By similarity.
FT   ACT_SITE    582    582       By similarity.
FT   DISULFID    671    702       By similarity.
FT   DISULFID    681    696       By similarity.
FT   DISULFID    866    961       By similarity.
FT   CONFLICT     14     14       K -> T (in Ref. 1; CAA31082).
FT   CONFLICT     25     25       C -> G (in Ref. 1; CAA31082).
FT   CONFLICT    503    503       S -> I (in Ref. 1; CAA31082).
FT   CONFLICT    507    507       S -> P (in Ref. 1; CAA31082).
FT   CONFLICT    555    555       L -> F (in Ref. 1; CAA31082).
FT   CONFLICT    894    894       G -> R (in Ref. 1; CAA31082).
FT   CONFLICT    951    951       A -> R (in Ref. 1; CAA31082).
SQ   SEQUENCE   962 AA;  100109 MW;  95212655950CB52A CRC64;
     MINRSVLKIP ALVKPLVQAL VLVGCTLGVA QAEVGNPRVN QLGYIPNGDR IAVYKASNNS
     AQTWQLTHNG SLIASGQTIP KGSDASSGDN IHHIDLSSVT ATGSGFTLTV GGDSSYPFSI
     SSTTFNAAFY DALKYFYHNR SGIAIETPYT GGGRGSYASH SRWSRPAGHL NQGANKGDMN
     VPCWSGTCNY SLNVTKGWYD AGDHGKYVVN GGISVWTLLN LYERAQHITG NLAAVADGSM
     NIPESGNGVA DILDEARWQM EFMLAMQVPQ GQAKAGMAHH KIHDVGWTGL PLAPHEDPQQ
     RALVPPSTAA TLNLAATAAQ AARIWKDIDA GFAALCLTAA ERAWNAAQAN PNDIYSGNYD
     NGGGGYGDRF VADEFYWAAA ELYITTGDSR YLPTINNYTL ERTDFGWPDT ELLGVMSLAV
     VPATHTNSLR IAARNHIQTI ASTHLTTQSA SGYPAPLSSL EYYWGSNSVI ANKLVLMGLA
     YDFSGNQNFA LGVSKGINYL FGSNVLSTSF ITGLGTNTVA QPHHRFWAGA LNSNYPWAPP
     GALSGGPNAG LEDSLSASRL SGCTSRPATC WLDSIDAWST NEITINWNAP LAWVLGFYND
     FAATQGGSSS SSSSSSSSVP VSSSSSSSII PSSSSSSIQP SSSSSSMPSS SSSSSSVVAS
     SSSSVSGGLR CNWYGTLYPL CVTTQSGWGW ENSQSCISAS TCSAQPAPYG IVGAASSSSQ
     AANRSPTLQL SANATGFEGG SMVCCTLHIN GAASDPDGDN LTYSWQVISG NTVVASGSSS
     SASIHVSNQR GYEVSMTVSD GRGGVATETT FVSVYFSDYF PGSSSSASNI NSSSSSSSSS
     SSSAIVSSSS SVVSSSSSSA ASGGNCQYVV TNQWNNGFTA VIRVRNNGSS AINGWSVNWS
     YSDGSRITNS WNANVTGNNP YAASALGWNA NIQPGQTAEF GFQGTKGAGS AQVPAVTGSV
     CQ
//
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