GUNA_CLOLO
ID GUNA_CLOLO Reviewed; 517 AA.
AC P54937;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=celA;
OS Clostridium longisporum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1523;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 49440 / B6405;
RX PubMed=8126442; DOI=10.1099/00221287-139-12-3233;
RA Mittendorf V., Thomson J.A.;
RT "Cloning of an endo-(1-->4)-beta-glucanase gene, celA, from the rumen
RT bacterium Clostridium sp. ('C. longisporum') and characterization of its
RT product, CelA, in Escherichia coli.";
RL J. Gen. Microbiol. 139:3233-3242(1993).
CC -!- FUNCTION: Hydrolyzes barley beta-glucan, lichenan,
CC carboxymethylcellulose and xylan. It shows preferential activity
CC against the larger cellooligosaccharides (cellohexaose and
CC cellopentaose); cellotetraose is the smallest substrate degraded
CC completely.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.8.;
CC Temperature dependence:
CC Optimum temperature is 43 degrees Celsius.;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; L02868; AAC37035.1; -; Unassigned_DNA.
DR PIR; I40798; I40798.
DR PDB; 6Q1I; X-ray; 1.35 A; A/B=27-382.
DR PDBsum; 6Q1I; -.
DR AlphaFoldDB; P54937; -.
DR SMR; P54937; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
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 InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..517
FT /note="Endoglucanase A"
FT /id="PRO_0000007849"
FT DOMAIN 416..517
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 26..?
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 382..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:6Q1I"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6Q1I"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6Q1I"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:6Q1I"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:6Q1I"
FT TURN 192..197
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 281..300
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 318..334
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:6Q1I"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:6Q1I"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:6Q1I"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:6Q1I"
SQ SEQUENCE 517 AA; 57660 MW; A1D1570302FFBA30 CRC64;
MKRSLLKTCS IIAGATIIFS SLSISRNPLE VQAASMRSAS EIVQEMGVGW NLGNTLDAKI
TNLSYNTSPI SFETGWGNPV TTKAMIDKIK NAGFKTIRIP TTWGEHLDGN NKLNEEWVKR
VKEVVDYCIA DDLYVILNTH HEGNWVIPTY AKESSVTPKL KTLWTQISEA FKDYDDHLIF
ETLNEPRLEG TPYEWTGGTS ESRDVVNKYN AAALESIRKT GGNNLSRAVM MPTYAASGSS
TTMNDFKVPD DKNVIASVHA YSPYFFAMDT SSNSVNTWGS SYDKYSLDVE LDSYLNTFKS
KGVPVVIGEF GSINKNNTSS RAELAEYYVT AAQKRGIPCV WWDNNYAETN KGETFGLLNR
STLNWYFSDI KDALIRGYKN VHPEATEDDK PSTDVTNPDS GNTKPDSGNT NPGTETTTPT
DNEKISITSK INDWGGAYQA DFTLKNNTSS DINNWSFKIK KNDIVFTNYW DVKITEENGY
YVVTPQAWKT TILANSSIVI SIQGTGKVIS NFEYKFD
