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 03-MAY-2023, entry version 96. 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; Bacillota; 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}. 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; 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 Gene3D; 3.20.20.80; Glycosidases; 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 PANTHER; PTHR31297:SF17; ENDOGLUCANASE; 1. DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF00150; Cellulase; 1. DR SMART; SM00637; CBD_II; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 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 //