GUNA_CELFI
ID GUNA_CELFI Reviewed; 449 AA.
AC P07984;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Endoglucanase A;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase A;
DE AltName: Full=Endo-1,4-beta-glucanase A;
DE Flags: Precursor;
GN Name=cenA;
OS Cellulomonas fimi.
OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX NCBI_TaxID=1708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023193; DOI=10.1016/0378-1119(86)90196-4;
RA Wong W.K.R., Gerhard B., Guo Z.M., Kilburn D.G., Warren R.A.J.,
RA Miller R.C. Jr.;
RT "Characterization and structure of an endoglucanase gene cenA of
RT Cellulomonas fimi.";
RL Gene 44:315-324(1986).
RN [2]
RP DOMAINS.
RX PubMed=2681184; DOI=10.1016/s0021-9258(19)84644-6;
RA Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.;
RT "Structural and functional analysis of a bacterial cellulase by
RT proteolysis.";
RL J. Biol. Chem. 264:17802-17808(1989).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=1761039; DOI=10.1111/j.1432-1033.1991.tb16384.x;
RA Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A.,
RA Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.;
RT "Structural and functional relationships in two families of beta-1,4-
RT glycanases.";
RL Eur. J. Biochem. 202:367-377(1991).
CC -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
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 -!- PTM: The linker region (also termed 'hinge') may be a potential site
CC for proteolysis.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; M15823; AAA23084.1; -; Genomic_DNA.
DR PIR; A24993; A24993.
DR AlphaFoldDB; P07984; -.
DR SMR; P07984; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR PRIDE; P07984; -.
DR SABIO-RK; P07984; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 32..449
FT /note="Endoglucanase A"
FT /id="PRO_0000007903"
FT DOMAIN 32..137
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 127..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..168
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 438..449
FT /note="Catalytic"
FT COMPBIAS 127..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 283
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 423
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT DISULFID 35..134
FT /evidence="ECO:0000269|PubMed:1761039"
FT DISULFID 248..291
FT /evidence="ECO:0000269|PubMed:1761039"
FT DISULFID 390..426
FT /evidence="ECO:0000269|PubMed:1761039"
SQ SEQUENCE 449 AA; 46731 MW; 67FF887814B3348D CRC64;
MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG ANVTITNLGD
PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN GSIPTGGTAS FGFNGSWAGS
NPTPASFSLN GTTCTGTVPT TSPTPTPTPT TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT
QGYRAWQAAS GTDKALLEKI ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV
YAIPGRDCGS HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF
LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS NYQTTADSKA
YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER PVAVNDGSGL DALLWVKLPG
ESDGACNGGP AAGQWWQEIA LEMARNARW
