GUN3_FIBSS
ID GUN3_FIBSS Reviewed; 658 AA.
AC P14250; C9RK83; D9S6Q5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Endoglucanase 3;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase 3;
DE AltName: Full=Endo-1,4-beta-glucanase 3;
DE Short=EG3;
DE Flags: Precursor;
GN Name=cel-3; OrderedLocusNames=Fisuc_2230, FSU_2772;
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; Fibrobacter.
OX NCBI_TaxID=59374;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 266-287.
RX PubMed=2676979; DOI=10.1128/jb.171.10.5587-5595.1989;
RA McGavin M.J., Forsberg C.W., Crosby B., Bell A.W., Dignard D., Thomas D.Y.;
RT "Structure of the cel-3 gene from Fibrobacter succinogenes S85 and
RT characteristics of the encoded gene product, endoglucanase 3.";
RL J. Bacteriol. 171:5587-5595(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Weimer P.J.,
RA Stevenson D.M., Boyum J., Brumm P.I., Mead D.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exhibits both endoglucanase and cellobiosidase activities.
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- PTM: May be a lipoprotein and may be glycosylated.
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; M29047; AAA24893.1; -; Genomic_DNA.
DR EMBL; CP001792; ACX75816.1; -; Genomic_DNA.
DR EMBL; CP002158; ADL25000.1; -; Genomic_DNA.
DR PIR; A33598; A33598.
DR RefSeq; WP_014546871.1; NC_017448.1.
DR AlphaFoldDB; P14250; -.
DR SMR; P14250; -.
DR STRING; 59374.Fisuc_2230; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PRIDE; P14250; -.
DR EnsemblBacteria; ADL25000; ADL25000; FSU_2772.
DR KEGG; fsc:FSU_2772; -.
DR KEGG; fsu:Fisuc_2230; -.
DR PATRIC; fig|59374.8.peg.2655; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_463623_0_0_0; -.
DR OMA; PDEANGH; -.
DR OrthoDB; 1395441at2; -.
DR Proteomes; UP000000517; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005087; CBM_fam11.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF03425; CBM_11; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Polysaccharide degradation; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 24..265
FT /evidence="ECO:0000269|PubMed:2676979"
FT /id="PRO_0000007861"
FT CHAIN 266..658
FT /note="Endoglucanase 3"
FT /id="PRO_0000007862"
FT DOMAIN 87..277
FT /note="CBM11"
FT /evidence="ECO:0000255"
FT REGION 42..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 448
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 597
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 658 AA; 73424 MW; 1C96E64C3F7109A6 CRC64;
MQLKNFYPKM SVLGIATVMA LTACGDENTQ ALFANNPVPG AENQVPVSSS DMSPTSSDAV
IDPTSSSAAV VDPSTLPAEG PITMPEGLGT LVDDFEDGDN LSKIGDYWYT YNDNDNGGAS
IITTPLNEEE NIIPGRVNNG SNYALQVNYT LDRGDYEYDP YVGWGVQVAP DEANGHFGGL
TYWYKGGAHE VHIEITDVED YDVHLAKFPA SRTWKQAVVR FKDLVQGGWG KEIPFDAKHI
MAISFQAKGN KSKLVTDSLF IDNIYLQDSS EVEKDQPDME IKDPVIPVVE FTEAEITVTN
PLQEKAMKYL NKGVNFTNWL ENADGKFKSF ELGESDVKIL ADNGFKSLRL PIDLDLYATN
RDAFIAGTDT ELKFDDDTLF LVLDSFVEWT AKYNMSFVID YHEYDNSYNT TSAKDPNYIK
MMAETWKHVA AHYAESPRED LFFELLNEPD MSDGKVTAAT WTTAAQAMID AIRTVDTKHT
ILFGDAQWYS ITLLAKRTPF TDDNIIYVIH TYEPFAFTHQ GGSWTDYATI HDIPFPYDPA
KWSTVSGDFG VNKSTKSYVK TNIKNYYKTG SKEAILEQIL KAKKWAATNN VPVIINEFGA
LNLRSTAESR LNYLTAMREI CDTLQIPWTH WGYTGNFSVI ENGKLIEGLD KALGVGSK
