GUNA_CELJU
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 25-MAY-2022, entry version 148.
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; Cellvibrionales;
OC Cellvibrionaceae; 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 Pseudomonas
RT 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 the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X12570; CAA31082.1; -; Genomic_DNA.
DR EMBL; CP000934; ACE85757.1; -; Genomic_DNA.
DR RefSeq; WP_012488069.1; NC_010995.1.
DR AlphaFoldDB; P10476; -.
DR SMR; 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 KEGG; cja:CJA_2472; -.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG4447; Bacteria.
DR eggNOG; COG5520; Bacteria.
DR HOGENOM; CLU_006010_3_0_6; -.
DR OrthoDB; 1226595at2; -.
DR Proteomes; UP000001036; Chromosome.
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 CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.30.32.30; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR036601; CBM10_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR009031; CBM_fam10.
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 InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
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; PS51763; CBM10; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..962
FT /note="Endoglucanase A"
FT /id="PRO_0000007957"
FT DOMAIN 670..699
FT /note="CBM10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT DOMAIN 859..962
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 608..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT DISULFID 671..702
FT /evidence="ECO:0000250"
FT DISULFID 681..696
FT /evidence="ECO:0000250"
FT DISULFID 866..961
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="K -> T (in Ref. 1; CAA31082)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="C -> G (in Ref. 1; CAA31082)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> I (in Ref. 1; CAA31082)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="S -> P (in Ref. 1; CAA31082)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="L -> F (in Ref. 1; CAA31082)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="G -> R (in Ref. 1; CAA31082)"
FT /evidence="ECO:0000305"
FT CONFLICT 951
FT /note="A -> R (in Ref. 1; CAA31082)"
FT /evidence="ECO:0000305"
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
