ID GUNC_CELFI STANDARD; PRT; 1101 AA. AC P14090; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 2. DT 21-MAR-2006, entry version 69. DE Endoglucanase C precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase C) DE (Cellulase C). GN Name=cenC; OS Cellulomonas fimi. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Cellulomonadaceae; Cellulomonas. OX NCBI_TaxID=1708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-42. RC STRAIN=ATCC 484; RX MEDLINE=92065819; PubMed=1956299; RA Coutinho J.B., Moser B., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.; RT "Nucleotide sequence of the endoglucanase C gene (cenC) of RT Cellulomonas fimi, its high-level expression in Escherichia coli, and RT characterization of its products."; RL Mol. Microbiol. 5:1221-1233(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64, AND PROTEIN SEQUENCE OF RP 625-641. RX MEDLINE=90103465; PubMed=2604391; RA Moser B., Gilkes N.R., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.; RT "Purification and characterization of endoglucanase C of Cellulomonas RT fimi, cloning of the gene, and analysis of in vivo transcripts of the RT gene."; RL Appl. Environ. Microbiol. 55:2480-2487(1989). RN [3] RP CELLULOSE-BINDING DOMAINS. RX MEDLINE=92269585; PubMed=1375311; RA Coutinho J.B., Gilkes N.R., Warren R.A.J., Kilburn D.G., RA Miller R.C. Jr.; RT "The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose RT and Sephadex is mediated by the N-terminal repeats."; RL Mol. Microbiol. 6:1243-1252(1992). RN [4] RP IDENTIFICATION OF IG-LIKE DOMAINS. RX MEDLINE=97035265; PubMed=8880921; RA Bateman A., Eddy S.R., Chothia C.; RT "Members of the immunoglobulin superfamily in bacteria."; RL Protein Sci. 5:1939-1942(1996). RN [5] RP STRUCTURE BY NMR OF 33-184. RX MEDLINE=97074498; PubMed=8916925; DOI=10.1021/bi961612s; RA Johnson P.E., Joshi M.D., Tomme P., Kilburn D.G., McIntosh L.P.; RT "Structure of the N-terminal cellulose-binding domain of Cellulomonas RT fimi CenC determined by nuclear magnetic resonance spectroscopy."; RL Biochemistry 35:14381-14394(1996). CC -!- FUNCTION: The biological conversion of cellulose to glucose CC generally requires three types of hydrolytic enzymes: (1) CC Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) CC Exocellobiohydrolases that cut the dissaccharide cellobiose from CC the nonreducing end of the cellulose polymer chain; (3) CC Beta-1,4-glucosidases which hydrolyze the cellobiose and other CC short cello-oligosaccharides to glucose. 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 2 CBM-cenC (cenC-type cellulose-binding) CC domains. CC -!- SIMILARITY: Contains 2 Ig-like (immunoglobulin-like) domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57858; CAA40993.1; -; Genomic_DNA. DR EMBL; M29707; AAA23087.1; ALT_TERM; Genomic_DNA. DR EMBL; M29708; AAA23088.1; ALT_SEQ; Genomic_DNA. DR PIR; S15271; S15271. DR PDB; 1CX1; NMR; A=178-328. DR PDB; 1GU3; X-ray; A=33-181. DR PDB; 1ULO; NMR; @=33-184. DR PDB; 1ULP; NMR; @=33-184. DR LinkHub; P14090; -. DR InterPro; IPR008928; 6hp_glycosidase. DR InterPro; IPR003305; CenC_carb_bd. DR InterPro; IPR008979; Gal_bd. DR InterPro; IPR001701; Glyco_hydro_9. DR InterPro; IPR004197; Glyco_hydro_9Ig. DR InterPro; IPR012343; Glyco_trans_sub. DR InterPro; IPR013098; I-set. DR InterPro; IPR003599; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013151; Immunoglobulin. DR Pfam; PF02018; CBM_4_9; 2. DR Pfam; PF02927; CelD_N; 1. DR Pfam; PF00759; Glyco_hydro_9; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF00047; ig; 1. DR SMART; SM00409; IG; 1. DR PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1; FALSE_NEG. DR PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1. DR PROSITE; PS50835; IG_LIKE; 1. KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Direct protein sequencing; Glycosidase; Hydrolase; KW Immunoglobulin domain; Polysaccharide degradation; Repeat; Signal. FT SIGNAL 1 32 FT CHAIN 33 1101 Endoglucanase C. FT /FTId=PRO_0000007946. FT DOMAIN 64 173 CBM-cenC 1. FT DOMAIN 212 318 CBM-cenC 2. FT DOMAIN 918 1006 Ig-like 1. FT DOMAIN 1008 1097 Ig-like 2. FT REGION 329 880 Catalytic. FT ACT_SITE 831 831 By similarity. FT ACT_SITE 882 882 By similarity. FT ACT_SITE 891 891 By similarity. FT TURN 42 43 FT TURN 46 47 FT STRAND 49 52 FT STRAND 54 55 FT STRAND 58 58 FT TURN 60 61 FT STRAND 62 68 FT TURN 70 71 FT TURN 74 75 FT STRAND 76 84 FT STRAND 86 86 FT TURN 88 89 FT STRAND 91 102 FT STRAND 104 105 FT STRAND 107 114 FT TURN 115 116 FT STRAND 119 123 FT STRAND 126 127 FT STRAND 129 130 FT STRAND 132 139 FT STRAND 141 142 FT STRAND 144 144 FT STRAND 146 147 FT STRAND 149 149 FT TURN 150 151 FT STRAND 152 152 FT STRAND 155 160 FT TURN 162 163 FT STRAND 164 164 FT STRAND 166 167 FT STRAND 169 180 FT STRAND 184 186 FT TURN 190 192 FT TURN 195 196 FT STRAND 198 203 FT STRAND 206 207 FT STRAND 209 210 FT STRAND 212 215 FT STRAND 218 218 FT STRAND 221 221 FT STRAND 223 223 FT TURN 224 225 FT STRAND 226 230 FT STRAND 235 235 FT TURN 237 238 FT STRAND 239 251 FT STRAND 253 260 FT STRAND 262 265 FT STRAND 269 270 FT STRAND 272 277 FT STRAND 279 279 FT STRAND 282 289 FT STRAND 292 292 FT STRAND 294 294 FT STRAND 296 299 FT STRAND 303 307 FT TURN 311 312 FT STRAND 315 324 SQ SEQUENCE 1101 AA; 115216 MW; 1FBAD189CC5F8B5D CRC64; MVSRRSSQAR GALTAVVATL ALALAGSGTA LAASPIGEGT FDDGPEGWVA YGTDGPLDTS TGALCVAVPA GSAQYGVGVV LNGVAIEEGT TYTLRYTATA STDVTVRALV GQNGAPYGTV LDTSPALTSE PRQVTETFTA SATYPATPAA DDPEGQIAFQ LGGFSADAWT FCLDDVALDS EVELLPHTSF AESLGPWSLY GTSEPVFADG RMCVDLPGGQ GNPWDAGLVY NGVPVGEGES YVLSFTASAT PDMPVRVLVG EGGGAYRTAF EQGSAPLTGE PATREYAFTS NLTFPPDGDA PGQVAFHLGK AGAYEFCISQ VSLTTSATPP PGYEPDTGPR VRVNQVGYLP FGPKRATLVT DAAEPVAWEL RDADGVVVAD GTSEPRGVEP SAAQAVHVLD FSDVTTQGAG YTLVADGETS RPFDIDGDLY QQLRYDALNY FYLARSGTEI EADVVGEEYA REAGHVGVAP NQGDTDVPCI GPRDYYDGWT CDYRLDVSGG WYDAGDHGKY VVNGGIAVGQ LLQTYERALH AGTADALADG TLDVPEHGND VPDVLDEARW ELEWMLSMIV PEGEYAGMVH HKVHDEGWTG LPLLPADDPQ ARSLHRPSTA ATLNLSAVAA QGARLLEPYD PQLAQTLLEA ARTTWAAAQE HPALYAPGEA GADGGGAYND SQVADEFYWA AAELYLTTGE DAFATAVTTS PLHTADVFTA DGFGWGSVAA LGRLDLATVP NELPGLDAVQ SSVVEGAQEY LAAQAGQGFG SLYSPPGGEY VWGSSSQVAN NLVVVATAYD LTGDERFRAA TLEGLDYLFG RNALNQSYVT GWGEVASHQQ HSRWFAHQLD PSLPSPPPGS LAGGPNSQAA TWDPTTKAAF PDGCAPSACY VDEIQAWSTN ELTVNWNSAL SWVASWVADQ GSAEPVPTAP VVTRQPVDAT VALGADATFT AEASGVPAPT VRWQVRAGRG WKDVAGATGT TLTVRATART DGTRYRAVFT NAAGSVESAV VRLTVERAAP VVTQHPADVR ARVGTRAVFR AAADGYPTPC VVWQVRWGGG SWRPIPWATS TTLSVPVTVL AAGTEYRAVF TNAVGTAATE PAELAVQRPR S //