Reviewed, UniProtKB/Swiss-Prot P16218 (GUNH_CLOTH)

Names and origin

Protein names

Recommended name:
    Endoglucanase H
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase H
      Short name=EgH
    Cellulase H

Gene names

Name:	celH
Ordered Locus Names:	Cthe_1472

Organism

Clostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]

Taxonomic identifier

203119 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	900 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 residues 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW substituted mannan metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: EC mannan endo-1,4-beta-mannosidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 44

44

Chain

45 – 900

856

Endoglucanase H

PRO_0000007854

Regions

Domain

655 – 900

246

CBM11

Repeat

833 – 856

24

1

Repeat

872 – 895

24

2

Region

45 – 630

586

Catalytic By similarity

Region

833 – 895

63

2 X 24 AA approximate repeats

Compositional bias

631 – 654

24

Pro/Thr-rich (linker)

Sites

Active site

460

1

Proton donor By similarity

Active site

565

1

Nucleophile By similarity

Secondary structure

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900

Helix Strand Turn

Details...

Beta strand

32 – 36

5

Helix

43 – 53

11

Beta strand

58 – 65

8

Helix

70 – 82

13

Beta strand

86 – 92

7

Helix

98 – 102

5

Turn

103 – 106

4

Helix

107 – 120

14

Beta strand

124 – 129

6

Beta strand

134 – 137

4

Helix

150 – 166

17

Beta strand

172 – 175

4

Beta strand

178 – 181

4

Helix

196 – 198

3

Beta strand

200 – 208

9

Helix

222 – 233

12

Beta strand

236 – 238

3

Beta strand

240 – 247

8

Helix

254 – 268

15

Beta strand

272 – 278

7

Beta strand

281 – 285

5

Helix

292 – 302

11

Beta strand

656 – 662

7

Beta strand

664 – 667

4

Beta strand

671 – 675

5

Beta strand

679 – 686

8

Beta strand

688 – 698

11

Beta strand

704 – 710

7

Beta strand

721 – 728

8

Beta strand

736 – 743

8

Beta strand

747 – 758

12

Beta strand

765 – 770

6

Helix

771 – 773

3

Beta strand

795 – 806

12

Beta strand

809 – 819

11

Sequences

	Sequence		Length	Mass (Da)
	P16218-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 973AFB1954FC246B	FASTA	900	102,416
	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

References

	« Hide 'large scale' referencesShow '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: 2197182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of Clostridium thermocellum ATCC 27405." 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. , 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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M31903 Genomic DNA. Translation: AAA23225.1.
CP000568 Genomic DNA. Translation: ABN52701.1.

PIR

JH0157.

RefSeq

YP_001037894.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V0A	X-ray	1.98	A	655-821	[»]
2BV9	X-ray	1.50	A	26-304	[»]
2BVD	X-ray	1.60	A	26-304	[»]
2CIP	X-ray	1.40	A	26-304	[»]
2CIT	X-ray	1.40	A	26-304	[»]
2V3G	X-ray	1.20	A	26-305	[»]
2VI0	X-ray	1.51	A	26-304	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM11. Carbohydrate-Binding Module Family 11.
GH26. Glycoside Hydrolase Family 26.
GH5. Glycoside Hydrolase Family 5.

Genome annotation databases

GeneID

4810622.

GenomeReviews

Gene locus Cthe_1472 in contig CP000568_GR.

KEGG

cth:Cthe_1472.

NMPDR

fig|203119.1.peg.2908.

Organism-specific databases

CMR

Search...

Phylogenomic databases

OMA

P16218. HATDENI.

Family and domain databases

InterPro

IPR005087. CBM_11.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_HAND_1.
IPR000805. Glyco_hydro_26.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.

Pfam

PF03425. CBM_11. 1 hit.
PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]

PROSITE

PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit. Uncertain.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUNH_CLOTH

Accession

Primary (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:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)