ID GUN4_THEFU STANDARD; PRT; 880 AA. AC P26221; Q08167; DT 01-MAY-1992 (Rel. 22, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Endoglucanase E-4 precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase E-4) DE (Cellulase E-4) (Cellulase E4). GN Name=celD; OS Thermomonospora fusca. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=2021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YX; RX MEDLINE=94028932; PubMed=8215374; RA Jung E.D., Lao G., Irwin D., Barr B.K., Benjamin A., Wilson D.B.; RT "DNA sequences and expression in Streptomyces lividans of an RT exoglucanase gene and an endoglucanase gene from Thermomonospora RT fusca."; RL Appl. Environ. Microbiol. 59:3032-3043(1993). RN [2] RP SEQUENCE REVISION. RA Wilson D.B.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP PARTIAL NUCLEOTIDE SEQUENCE. RC STRAIN=YX; RX MEDLINE=91258320; PubMed=1904434; RA Lao G., Ghangas G.S., Jung E.D., Wilson D.B.; RT "DNA sequences of three beta-1,4-endoglucanase genes from RT Thermomonospora fusca."; RL J. Bacteriol. 173:3397-3407(1991). RN [4] RP PROTEIN SEQUENCE OF 47-67. RA Wilson D.B.; RT "Cellulases of Thermomonospora fusca."; RL Meth. Enzymol. 160:314-323(1988). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-651. RX MEDLINE=97475222; PubMed=9334746; RA Sakon J., Irwin D., Wilson D.B., Karplus P.A.; RT "Structure and mechanism of endo/exocellulase E4 from Thermomonospora RT fusca."; RL Nat. Struct. Biol. 4:810-818(1997). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic CC linkages in cellulose, lichenin and cereal beta-D-glucans. CC -!- PATHWAY: Cellulose degradation. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) CC family. CC -!- SIMILARITY: Contains 1 fibronectin type III domain. CC -!- SIMILARITY: Contains 1 fungal-type cellulose-binding (CBD) domain. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; L20093; AAB42155.1; -. DR PIR; B42360; B42360. DR PDB; 1JS4; X-ray; A/B=47-651. DR PDB; 1TF4; X-ray; A/B=47-651. DR PDB; 3TF4; X-ray; A/B=47-651. DR PDB; 4TF4; X-ray; A/B=47-651. DR InterPro; IPR001919; Bac_celose-bind. DR InterPro; IPR001956; CBD_3. DR InterPro; IPR008965; Cellul_bind. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR001701; Glyco_hydro_9. DR InterPro; IPR008928; Glyco_trans_6hp. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF00942; CBM_3; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF00759; Glyco_hydro_9; 1. DR ProDom; PD001947; CBD_3; 1. DR SMART; SM00637; CBD_II; 1. DR SMART; SM00060; FN3; 1. DR PROSITE; PS00561; CBD_BACTERIAL; 1. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1; 1. DR PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1. KW 3D-structure; Cellulose degradation; Direct protein sequencing; KW Glycosidase; Hydrolase; Signal. FT SIGNAL 1 46 FT CHAIN 47 880 Endoglucanase E-4. FT DOMAIN 675 766 Fibronectin type-III. FT DOMAIN 776 880 Cellulose-binding. FT ACT_SITE 427 427 By similarity. FT ACT_SITE 461 461 By similarity. FT ACT_SITE 470 470 By similarity. FT HELIX 52 65 FT TURN 66 66 FT STRAND 67 67 FT STRAND 69 69 FT TURN 73 74 FT TURN 78 79 FT STRAND 83 83 FT TURN 85 88 FT HELIX 89 91 FT TURN 92 92 FT STRAND 99 99 FT STRAND 107 108 FT HELIX 109 125 FT HELIX 127 132 FT TURN 133 134 FT HELIX 136 152 FT TURN 153 153 FT STRAND 156 156 FT TURN 157 158 FT STRAND 159 164 FT HELIX 167 172 FT HELIX 177 179 FT STRAND 186 190 FT TURN 191 192 FT STRAND 193 193 FT HELIX 196 213 FT TURN 214 216 FT HELIX 218 237 FT HELIX 242 244 FT TURN 245 245 FT TURN 247 248 FT HELIX 249 252 FT HELIX 259 273 FT HELIX 276 285 FT HELIX 286 288 FT STRAND 291 291 FT TURN 293 294 FT STRAND 298 298 FT HELIX 310 321 FT HELIX 324 336 FT TURN 337 339 FT STRAND 341 341 FT TURN 342 343 FT STRAND 344 344 FT STRAND 348 348 FT TURN 350 351 FT STRAND 354 354 FT HELIX 361 378 FT HELIX 382 400 FT TURN 401 401 FT TURN 404 405 FT STRAND 410 410 FT TURN 411 412 FT HELIX 424 427 FT TURN 428 428 FT TURN 434 435 FT TURN 445 446 FT STRAND 448 448 FT TURN 455 456 FT TURN 463 464 FT TURN 466 469 FT HELIX 473 476 FT HELIX 477 490 FT STRAND 509 517 FT STRAND 522 531 FT TURN 535 536 FT STRAND 540 540 FT STRAND 543 550 FT TURN 553 554 FT HELIX 557 559 FT STRAND 561 563 FT STRAND 567 567 FT STRAND 576 577 FT TURN 580 581 FT STRAND 582 588 FT TURN 590 591 FT STRAND 594 594 FT TURN 599 602 FT STRAND 603 611 FT TURN 614 615 FT HELIX 618 620 FT HELIX 622 624 FT TURN 625 626 FT STRAND 632 633 FT TURN 635 636 FT STRAND 638 641 FT TURN 642 643 FT STRAND 644 647 SQ SEQUENCE 880 AA; 95203 MW; 5EA9A6ABF45A4D9A CRC64; MSVTEPPPRR RGRHSRARRF LTSLGATAAL TAGMLGVPLA TGTAHAEPAF NYAEALQKSM FFYEAQRSGK LPENNRVSWR GDSGLNDGAD VGLDLTGGWY DAGDHVKFGF PMAFTATMLA WGAIESPEGY IRSGQMPYLK DNLRWVNDYF IKAHPSPNVL YVQVGDGDAD HKWWGPAEVM PMERPSFKVD PSCPGSDVAA ETAAAMAASS IVFADDDPAY AATLVQHAKQ LYTFADTYRG VYSDCVPAGA FYNSWSGYQD ELVWGAYWLY KATGDDSYLA KAEYEYDFLS TEQQTDLRSY RWTIAWDDKS YGTYVLLAKE TGKQKYIDDA NRWLDYWTVG VNGQRVPYSP GGMAVLDTWG ALRYAANTAF VALVYAKVID DPVRKQRYHD FAVRQINYAL GDNPRNSSYV VGFGNNPPRN PHHRTAHGSW TDSIASPAEN RHVLYGALVG GPGSPNDAYT DDRQDYVANE VATDYNAGFS SALAMLVEEY GGTPLADFPP TEEPDGPEIF VEAQINTPGT TFTEIKAMIR NQSGWPARML DKGTFRYWFT LDEGVDPADI TVSSAYNQCA TPEDVHHVSG DLYYVEIDCT GEKIFPGGQS EHRREVQFRI AGGPGWDPSN DWSFQGIGNE LAPAPYIVLY DDGVPVWGTA PEEGEEPGGG EGPGGGEEPG EDVTPPSAPG SPAVRDVTST SAVLTWSASS DTGGSGVAGY DVFLRAGTGQ EQKVGSTTRT SFTLTGLEPD TTYIAAVVAR DNAGNVSQRS TVSFTTLAEN GGGPDASCTV GYSTNDWDSG FTASIRITYH GTAPLSSWEL SFTFPAGQQV THGWNATWRQ DGAAVTATPM SWNSSLAPGA TVEVGFNGSW SGSNTPPTDF TLNGEPCALA //