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Protein

Endoglucanase 3

Gene

cel-3

Organism
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits both endoglucanase and cellobiosidase activities.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei448 – 4481Proton donorBy similarity
Active sitei597 – 5971NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 3 (EC:3.2.1.4)
Alternative name(s):
Cellulase 3
Endo-1,4-beta-glucanase 3
Short name:
EG3
Gene namesi
Name:cel-3
Ordered Locus Names:Fisuc_2230, FSU_2772
OrganismiFibrobacter succinogenes (strain ATCC 19169 / S85)
Taxonomic identifieri59374 [NCBI]
Taxonomic lineageiBacteriaFibrobacteresFibrobacteralesFibrobacteraceaeFibrobacter
ProteomesiUP000001497 Componenti: Chromosome UP000000517 Componenti: Chromosome

Subcellular locationi

Membrane Curated; Lipid-anchor PROSITE-ProRule annotation

GO - Cellular componenti

  1. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323PROSITE-ProRule annotationAdd
BLAST
Propeptidei24 – 2652421 PublicationPRO_0000007861Add
BLAST
Chaini266 – 658393Endoglucanase 3PRO_0000007862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi24 – 241N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi24 – 241S-diacylglycerol cysteinePROSITE-ProRule annotation

Post-translational modificationi

May be a lipoprotein and may be glycosylated.

Keywords - PTMi

Lipoprotein, Palmitate, Zymogen

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi59374.Fisuc_2230.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
OMAiDEANGHF.
OrthoDBiEOG6NPM7N.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005087. CBM_fam11.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03425. CBM_11. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 2 hits.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLKNFYPKM SVLGIATVMA LTACGDENTQ ALFANNPVPG AENQVPVSSS
60 70 80 90 100
DMSPTSSDAV IDPTSSSAAV VDPSTLPAEG PITMPEGLGT LVDDFEDGDN
110 120 130 140 150
LSKIGDYWYT YNDNDNGGAS IITTPLNEEE NIIPGRVNNG SNYALQVNYT
160 170 180 190 200
LDRGDYEYDP YVGWGVQVAP DEANGHFGGL TYWYKGGAHE VHIEITDVED
210 220 230 240 250
YDVHLAKFPA SRTWKQAVVR FKDLVQGGWG KEIPFDAKHI MAISFQAKGN
260 270 280 290 300
KSKLVTDSLF IDNIYLQDSS EVEKDQPDME IKDPVIPVVE FTEAEITVTN
310 320 330 340 350
PLQEKAMKYL NKGVNFTNWL ENADGKFKSF ELGESDVKIL ADNGFKSLRL
360 370 380 390 400
PIDLDLYATN RDAFIAGTDT ELKFDDDTLF LVLDSFVEWT AKYNMSFVID
410 420 430 440 450
YHEYDNSYNT TSAKDPNYIK MMAETWKHVA AHYAESPRED LFFELLNEPD
460 470 480 490 500
MSDGKVTAAT WTTAAQAMID AIRTVDTKHT ILFGDAQWYS ITLLAKRTPF
510 520 530 540 550
TDDNIIYVIH TYEPFAFTHQ GGSWTDYATI HDIPFPYDPA KWSTVSGDFG
560 570 580 590 600
VNKSTKSYVK TNIKNYYKTG SKEAILEQIL KAKKWAATNN VPVIINEFGA
610 620 630 640 650
LNLRSTAESR LNYLTAMREI CDTLQIPWTH WGYTGNFSVI ENGKLIEGLD

KALGVGSK
Length:658
Mass (Da):73,424
Last modified:February 1, 1996 - v2
Checksum:i1C96E64C3F7109A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29047 Genomic DNA. Translation: AAA24893.1.
CP001792 Genomic DNA. Translation: ACX75816.1.
CP002158 Genomic DNA. Translation: ADL25000.1.
PIRiA33598.
RefSeqiWP_014546871.1. NC_017448.1.
YP_003250298.1. NC_013410.1.
YP_005822586.1. NC_017448.1.

Genome annotation databases

EnsemblBacteriaiACX75816; ACX75816; Fisuc_2230.
ADL25000; ADL25000; FSU_2772.
KEGGifsc:FSU_2772.
fsu:Fisuc_2230.
PATRICi32144235. VBIFibSuc28982_2179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29047 Genomic DNA. Translation: AAA24893.1.
CP001792 Genomic DNA. Translation: ACX75816.1.
CP002158 Genomic DNA. Translation: ADL25000.1.
PIRiA33598.
RefSeqiWP_014546871.1. NC_017448.1.
YP_003250298.1. NC_013410.1.
YP_005822586.1. NC_017448.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi59374.Fisuc_2230.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACX75816; ACX75816; Fisuc_2230.
ADL25000; ADL25000; FSU_2772.
KEGGifsc:FSU_2772.
fsu:Fisuc_2230.
PATRICi32144235. VBIFibSuc28982_2179.

Phylogenomic databases

eggNOGiCOG2730.
OMAiDEANGHF.
OrthoDBiEOG6NPM7N.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005087. CBM_fam11.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03425. CBM_11. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 2 hits.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the cel-3 gene from Fibrobacter succinogenes S85 and characteristics of the encoded gene product, endoglucanase 3."
    McGavin M.J., Forsberg C.W., Crosby B., Bell A.W., Dignard D., Thomas D.Y.
    J. Bacteriol. 171:5587-5595(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 266-287.
  2. "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Weimer P.J.
    , Stevenson D.M., Boyum J., Brumm P.I., Mead D.
    Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19169 / S85.
  3. "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85."
    Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B., Russell J.B., Cann I.K.O., Mackie R.I., White B.A.
    Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19169 / S85.

Entry informationi

Entry nameiGUN3_FIBSS
AccessioniPrimary (citable) accession number: P14250
Secondary accession number(s): C9RK83, D9S6Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: April 1, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.