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Protein

Endoglucanase H

Gene

celH

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei131Proton donorPROSITE-ProRule annotation1
Active sitei244NucleophilePROSITE-ProRule annotation1
Active sitei460Proton donorBy similarity1
Active sitei565NucleophileBy similarity1

GO - Molecular functioni

  • cellulase activity Source: MENGO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16422.

Protein family/group databases

CAZyiCBM11. Carbohydrate-Binding Module Family 11.
GH26. Glycoside Hydrolase Family 26.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase H (EC:3.2.1.4)
Alternative name(s):
Cellulase H
Endo-1,4-beta-glucanase H
Short name:
EgH
Gene namesi
Name:celH
Ordered Locus Names:Cthe_1472
OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
Proteomesi
  • UP000002145 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44Add BLAST44
ChainiPRO_000000785445 – 900Endoglucanase HAdd BLAST856

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_1472.

Structurei

Secondary structure

1900
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 36Combined sources5
Helixi43 – 53Combined sources11
Beta strandi58 – 65Combined sources8
Helixi70 – 82Combined sources13
Beta strandi86 – 92Combined sources7
Helixi98 – 102Combined sources5
Turni103 – 106Combined sources4
Helixi107 – 120Combined sources14
Beta strandi124 – 129Combined sources6
Beta strandi134 – 137Combined sources4
Helixi150 – 166Combined sources17
Beta strandi172 – 175Combined sources4
Beta strandi178 – 181Combined sources4
Helixi196 – 198Combined sources3
Beta strandi200 – 208Combined sources9
Turni214 – 216Combined sources3
Helixi222 – 233Combined sources12
Beta strandi236 – 238Combined sources3
Beta strandi240 – 247Combined sources8
Helixi254 – 268Combined sources15
Beta strandi272 – 278Combined sources7
Beta strandi281 – 285Combined sources5
Helixi292 – 301Combined sources10
Helixi329 – 336Combined sources8
Beta strandi338 – 341Combined sources4
Beta strandi348 – 350Combined sources3
Beta strandi353 – 355Combined sources3
Helixi360 – 369Combined sources10
Beta strandi373 – 376Combined sources4
Helixi381 – 383Combined sources3
Helixi394 – 409Combined sources16
Beta strandi413 – 417Combined sources5
Helixi423 – 426Combined sources4
Helixi428 – 445Combined sources18
Turni446 – 448Combined sources3
Beta strandi453 – 456Combined sources4
Beta strandi463 – 465Combined sources3
Helixi467 – 484Combined sources18
Beta strandi490 – 497Combined sources8
Beta strandi502 – 504Combined sources3
Beta strandi512 – 520Combined sources9
Helixi524 – 527Combined sources4
Helixi537 – 557Combined sources21
Beta strandi561 – 566Combined sources6
Beta strandi571 – 573Combined sources3
Helixi574 – 590Combined sources17
Beta strandi594 – 597Combined sources4
Helixi606 – 608Combined sources3
Beta strandi612 – 614Combined sources3
Turni615 – 618Combined sources4
Helixi622 – 628Combined sources7
Beta strandi656 – 662Combined sources7
Beta strandi664 – 667Combined sources4
Beta strandi671 – 675Combined sources5
Beta strandi679 – 686Combined sources8
Beta strandi688 – 698Combined sources11
Beta strandi704 – 710Combined sources7
Beta strandi721 – 728Combined sources8
Beta strandi730 – 732Combined sources3
Beta strandi736 – 743Combined sources8
Beta strandi747 – 758Combined sources12
Beta strandi765 – 770Combined sources6
Helixi771 – 773Combined sources3
Beta strandi788 – 790Combined sources3
Beta strandi795 – 806Combined sources12
Beta strandi809 – 819Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4U3AX-ray2.42A/B290-654[»]
4U5IX-ray2.50A/B290-654[»]
4U5KX-ray2.65A/B290-654[»]
5BYWX-ray2.60A/B/C/D/E290-654[»]
ProteinModelPortaliP16218.
SMRiP16218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16218.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 298GH26PROSITE-ProRule annotationAdd BLAST254
Domaini655 – 900CBM11Add BLAST246
Domaini827 – 900DockerinPROSITE-ProRule annotationAdd BLAST74

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni300 – 630CatalyticBy similarityAdd BLAST331

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi631 – 654Pro/Thr-rich (linker)Add BLAST24

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 26 family.Curated
Contains 1 dockerin domain.PROSITE-ProRule annotation
Contains 1 GH26 (glycosyl hydrolase family 26) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108K2F. Bacteria.
COG2730. LUCA.
COG4124. LUCA.
KOiK01179.
OMAiGSANEIR.
OrthoDBiPOG091H0FI3.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR005087. CBM_fam11.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR008979. Galactose-bd-like.
IPR022790. GH26_dom.
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.
PF00404. Dockerin_1. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS51764. GH26. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRLLVSFL VLSIIVGLLS FQSLGNYNSG LKIGAWVGTQ PSESAIKSFQ
60 70 80 90 100
ELQGRKLDIV HQFINWSTDF SWVRPYADAV YNNGSILMIT WEPWEYNTVD
110 120 130 140 150
IKNGKADAYI TRMAQDMKAY GKEIWLRPLH EANGDWYPWA IGYSSRVNTN
160 170 180 190 200
ETYIAAFRHI VDIFRANGAT NVKWVFNVNC DNVGNGTSYL GHYPGDNYVD
210 220 230 240 250
YTSIDGYNWG TTQSWGSQWQ SFDQVFSRAY QALASINKPI IIAEFASAEI
260 270 280 290 300
GGNKARWITE AYNSIRTSYN KVIAAVWFHE NKETDWRINS SPEALAAYRE
310 320 330 340 350
AIGAGSSNPT PTPTWTSTPP SSSPKAVDPF EMVRKMGMGT NLGNTLEAPY
360 370 380 390 400
EGSWSKSAME YYFDDFKAAG YKNVRIPVRW DNHTMRTYPY TIDKAFLDRV
410 420 430 440 450
EQVVDWSLSR GFVTIINSHH DDWIKEDYNG NIERFEKIWE QIAERFKNKS
460 470 480 490 500
ENLLFEIMNE PFGNITDEQI DDMNSRILKI IRKTNPTRIV IIGGGYWNSY
510 520 530 540 550
NTLVNIKIPD DPYLIGTFHY YDPYEFTHKW RGTWGTQEDM DTVVRVFDFV
560 570 580 590 600
KSWSDRNNIP VYFGEFAVMA YADRTSRVKW YDFISDAALE RGFACSVWDN
610 620 630 640 650
GVFGSLDNDM AIYNRDTRTF DTEILNALFN PGTYPSYSPK PSPTPRPTKP
660 670 680 690 700
PVTPAVGEKM LDDFEGVLNW GSYSGEGAKV STKIVSGKTG NGMEVSYTGT
710 720 730 740 750
TDGYWGTVYS LPDGDWSKWL KISFDIKSVD GSANEIRFMI AEKSINGVGD
760 770 780 790 800
GEHWVYSITP DSSWKTIEIP FSSFRRRLDY QPPGQDMSGT LDLDNIDSIH
810 820 830 840 850
FMYANNKSGK FVVDNIKLIG ATSDPTPSIK HGDLNFDNAV NSTDLLMLKR
860 870 880 890 900
YILKSLELGT SEQEEKFKKA ADLNRDNKVD STDLTILKRY LLKAISEIPI
Length:900
Mass (Da):102,416
Last modified:April 1, 1990 - v1
Checksum:i973AFB1954FC246B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31903 Genomic DNA. Translation: AAA23225.1.
CP000568 Genomic DNA. Translation: ABN52701.1.
PIRiJH0157.
RefSeqiWP_011838089.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN52701; ABN52701; Cthe_1472.
KEGGicth:Cthe_1472.
PATRICi19516761. VBICloThe47081_1560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31903 Genomic DNA. Translation: AAA23225.1.
CP000568 Genomic DNA. Translation: ABN52701.1.
PIRiJH0157.
RefSeqiWP_011838089.1. NC_009012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4U3AX-ray2.42A/B290-654[»]
4U5IX-ray2.50A/B290-654[»]
4U5KX-ray2.65A/B290-654[»]
5BYWX-ray2.60A/B/C/D/E290-654[»]
ProteinModelPortaliP16218.
SMRiP16218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203119.Cthe_1472.

Protein family/group databases

CAZyiCBM11. Carbohydrate-Binding Module Family 11.
GH26. Glycoside Hydrolase Family 26.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN52701; ABN52701; Cthe_1472.
KEGGicth:Cthe_1472.
PATRICi19516761. VBICloThe47081_1560.

Phylogenomic databases

eggNOGiENOG4108K2F. Bacteria.
COG2730. LUCA.
COG4124. LUCA.
KOiK01179.
OMAiGSANEIR.
OrthoDBiPOG091H0FI3.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16422.

Miscellaneous databases

EvolutionaryTraceiP16218.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR005087. CBM_fam11.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR008979. Galactose-bd-like.
IPR022790. GH26_dom.
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.
PF00404. Dockerin_1. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS51764. GH26. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUNH_CLOTH
AccessioniPrimary (citable) accession number: P16218
Secondary accession number(s): A3DFH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.