GUNI_ACET2
ID GUNI_ACET2 Reviewed; 887 AA.
AC Q02934; A3DBF2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Endoglucanase 1;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase I;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE AltName: Full=Endoglucanase I;
DE Short=EGI;
DE Flags: Precursor;
GN Name=celI; OrderedLocusNames=Cthe_0040;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 56-69.
RX PubMed=8436949; DOI=10.1099/00221287-139-2-307;
RA Hazlewood G.P., Davidson K., Laurie J.I., Huskisson N.S., Gilbert H.J.;
RT "Gene sequence and properties of CelI, a family E endoglucanase from
RT Clostridium thermocellum.";
RL J. Gen. Microbiol. 139:307-316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-
CC glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
CC Principally active against barley beta-glucan.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- INTERACTION:
CC Q02934; Q02934: celI; NbExp=4; IntAct=EBI-8601842, EBI-8601842;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR EMBL; L04735; AAA20892.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN51281.1; -; Genomic_DNA.
DR PIR; A47704; A47704.
DR RefSeq; WP_011837740.1; NC_009012.1.
DR PDB; 2XFG; X-ray; 1.68 A; A=54-516, B=517-683.
DR PDBsum; 2XFG; -.
DR AlphaFoldDB; Q02934; -.
DR SMR; Q02934; -.
DR MINT; Q02934; -.
DR STRING; 203119.Cthe_0040; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PRIDE; Q02934; -.
DR EnsemblBacteria; ABN51281; ABN51281; Cthe_0040.
DR KEGG; cth:Cthe_0040; -.
DR eggNOG; COG4447; Bacteria.
DR eggNOG; COG4733; Bacteria.
DR HOGENOM; CLU_008926_0_2_9; -.
DR OMA; RWLDYWT; -.
DR OrthoDB; 1226595at2; -.
DR UniPathway; UPA00696; -.
DR EvolutionaryTrace; Q02934; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.710; -; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR Pfam; PF00942; CBM_3; 2.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01067; CBM_3; 2.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49384; SSF49384; 2.
DR PROSITE; PS51172; CBM3; 2.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT SIGNAL 1..55
FT /evidence="ECO:0000269|PubMed:8436949"
FT CHAIN 56..887
FT /note="Endoglucanase 1"
FT /id="PRO_0000007951"
FT DOMAIN 529..684
FT /note="CBM3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT DOMAIN 736..887
FT /note="CBM3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT REGION 40..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..518
FT /note="Catalytic"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CONFLICT 861..887
FT /note="NPSASDYTDWNRVTLYISNKLVYGKEP -> KQACLRQRTLIYLYATWLR
FT (in Ref. 1; AAA20892)"
FT /evidence="ECO:0000305"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 223..239
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 245..265
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 273..277
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 285..299
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 336..347
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 352..364
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 388..403
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 410..428
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 498..515
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 533..544
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 547..556
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 565..575
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 611..617
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:2XFG"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 631..640
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:2XFG"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:2XFG"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:2XFG"
SQ SEQUENCE 887 AA; 98531 MW; E587626445BA7A95 CRC64;
MRLVNSLGRR KILLILAVIV AFSTVLLFAK LWGRKTSSTL DEVGSKTHGD LTAENKNGGY
LPEEEIPDQP PATGAFNYGE ALQKAIFFYE CQRSGKLDPS TLRLNWRGDS GLDDGKDAGI
DLTGGWYDAG DHVKFNLPMS YSAAMLGWAV YEYEDAFKQS GQYNHILNNI KWACDYFIKC
HPEKDVYYYQ VGDGHADHAW WGPAEVMPME RPSYKVDRSS PGSTVVAETS AALAIASIIF
KKVDGEYSKE CLKHAKELFE FADTTKSDDG YTAANGFYNS WSGFYDELSW AAVWLYLATN
DSSYLDKAES YSDKWGYEPQ TNIPKYKWAQ CWDDVTYGTY LLLARIKNDN GKYKEAIERH
LDWWTTGYNG ERITYTPKGL AWLDQWGSLR YATTTAFLAC VYSDWENGDK EKAKTYLEFA
RSQADYALGS TGRSFVVGFG ENPPKRPHHR TAHGSWADSQ MEPPEHRHVL YGALVGGPDS
TDNYTDDISN YTCNEVACDY NAGFVGLLAK MYKLYGGSPD PKFNGIEEVP EDEIFVEAGV
NASGNNFIEI KAIVNNKSGW PARVCENLSF RYFINIEEIV NAGKSASDLQ VSSSYNQGAK
LSDVKHYKDN IYYVEVDLSG TKIYPGGQSA YKKEVQFRIS APEGTVFNPE NDYSYQGLSA
GTVVKSEYIP VYDAGVLVFG REPGSASKST SKDNGLSKAT PTVKTESQPT AKHTQNPASD
FKTPANQNSV KKDQGIKGEV VLQYANGNAG ATSNSINPRF KIINNGTKAI NLSDVKIRYY
YTKEGGASQN FWCDWSSAGN SNVTGNFFNL SSPKEGADTC LEVGFGSGAG TLDPGGSVEV
QIRFSKEDWS NYNQSNDYSF NPSASDYTDW NRVTLYISNK LVYGKEP
