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P16218 (GUNH_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase H
EC=3.2.1.4
Alternative name(s):
Cellulase H
Endo-1,4-beta-glucanase H
Short name=EgH
Gene names
Name:celH
Ordered Locus Names:Cthe_1472
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length900 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Catalytic activity

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

Domain

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similarities

In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.

In the C-terminal section; belongs to the glycosyl hydrolase 26 family.

Contains 1 CBM11 (carbohydrate binding type-11) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4444
Chain45 – 900856Endoglucanase H
PRO_0000007854

Regions

Domain655 – 900246CBM11
Repeat833 – 856241
Repeat872 – 895242
Region45 – 630586Catalytic By similarity
Region833 – 895632 X 24 AA approximate repeats
Compositional bias631 – 65424Pro/Thr-rich (linker)

Sites

Active site4601Proton donor By similarity
Active site5651Nucleophile By similarity

Secondary structure

1 .......................................................................... 900
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16218 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 973AFB1954FC246B

FASTA900102,416
        10         20         30         40         50         60 
MKKRLLVSFL VLSIIVGLLS FQSLGNYNSG LKIGAWVGTQ PSESAIKSFQ ELQGRKLDIV 

        70         80         90        100        110        120 
HQFINWSTDF SWVRPYADAV YNNGSILMIT WEPWEYNTVD IKNGKADAYI TRMAQDMKAY 

       130        140        150        160        170        180 
GKEIWLRPLH EANGDWYPWA IGYSSRVNTN ETYIAAFRHI VDIFRANGAT NVKWVFNVNC 

       190        200        210        220        230        240 
DNVGNGTSYL GHYPGDNYVD YTSIDGYNWG TTQSWGSQWQ SFDQVFSRAY QALASINKPI 

       250        260        270        280        290        300 
IIAEFASAEI GGNKARWITE AYNSIRTSYN KVIAAVWFHE NKETDWRINS SPEALAAYRE 

       310        320        330        340        350        360 
AIGAGSSNPT PTPTWTSTPP SSSPKAVDPF EMVRKMGMGT NLGNTLEAPY EGSWSKSAME 

       370        380        390        400        410        420 
YYFDDFKAAG YKNVRIPVRW DNHTMRTYPY TIDKAFLDRV EQVVDWSLSR GFVTIINSHH 

       430        440        450        460        470        480 
DDWIKEDYNG NIERFEKIWE QIAERFKNKS ENLLFEIMNE PFGNITDEQI DDMNSRILKI 

       490        500        510        520        530        540 
IRKTNPTRIV IIGGGYWNSY NTLVNIKIPD DPYLIGTFHY YDPYEFTHKW RGTWGTQEDM 

       550        560        570        580        590        600 
DTVVRVFDFV KSWSDRNNIP VYFGEFAVMA YADRTSRVKW YDFISDAALE RGFACSVWDN 

       610        620        630        640        650        660 
GVFGSLDNDM AIYNRDTRTF DTEILNALFN PGTYPSYSPK PSPTPRPTKP PVTPAVGEKM 

       670        680        690        700        710        720 
LDDFEGVLNW GSYSGEGAKV STKIVSGKTG NGMEVSYTGT TDGYWGTVYS LPDGDWSKWL 

       730        740        750        760        770        780 
KISFDIKSVD GSANEIRFMI AEKSINGVGD GEHWVYSITP DSSWKTIEIP FSSFRRRLDY 

       790        800        810        820        830        840 
QPPGQDMSGT LDLDNIDSIH FMYANNKSGK FVVDNIKLIG ATSDPTPSIK HGDLNFDNAV 

       850        860        870        880        890        900 
NSTDLLMLKR YILKSLELGT SEQEEKFKKA ADLNRDNKVD STDLTILKRY LLKAISEIPI

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and deletion analysis of the cellulase-encoding gene celH of Clostridium thermocellum."
Yaguee E., Beguin P., Aubert J.-P.
Gene 89:61-67(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Clostridium thermocellum ATCC 27405."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M31903 Genomic DNA. Translation: AAA23225.1.
CP000568 Genomic DNA. Translation: ABN52701.1.
PIRJH0157.
RefSeqYP_001037894.1. NC_009012.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0AX-ray1.98A655-821[»]
2BV9X-ray1.50A26-304[»]
2BVDX-ray1.60A26-304[»]
2CIPX-ray1.40A26-304[»]
2CITX-ray1.40A26-304[»]
2LRONMR-A655-821[»]
2LRPNMR-A655-821[»]
2V3GX-ray1.20A26-305[»]
2VI0X-ray1.51A26-304[»]
ProteinModelPortalP16218.
SMRP16218. Positions 29-304, 655-821.
ModBaseSearch...

Protein-protein interaction databases

STRING203119.Cthe_1472.

Protein family/group databases

CAZyCBM11. Carbohydrate-Binding Module Family 11.
GH26. Glycoside Hydrolase Family 26.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN52701; ABN52701; Cthe_1472.
GeneID4810622.
KEGGcth:Cthe_1472.
PATRIC19516761. VBICloThe47081_1560.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2730.
KOK01179.
OMAGSANEIR.
ProtClustDBCLSK625314.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-1525-MONOMER.
MetaCyc:MONOMER-16422.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
3.20.20.80. 2 hits.
InterProIPR005087. CBM_fam11.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF03425. CBM_11. 1 hit.
PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
SUPFAMSSF63446. Cellulos_enz_dockerin_1. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF51445. Glyco_hydro_cat. 2 hits.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit. Uncertain.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16218.

Entry information

Entry nameGUNH_CLOTH
AccessionPrimary (citable) accession number: P16218
Secondary accession number(s): A3DFH2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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