Reviewed, UniProtKB/Swiss-Prot P25472 (GUND_CLOCE)

Names and origin

Protein names

Recommended name:
    Endoglucanase D
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase D
    Cellulase D
    EGCCD

Gene names

Name:	celCCD
Ordered Locus Names:	Ccel_0840

Organism

Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)

Taxonomic identifier

394503 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	584 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pathway	Glycan metabolism; cellulose degradation.
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	Belongs to the glycosyl hydrolase 5 (cellulase A) 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
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 584	560	Endoglucanase D		PRO_0000007846
Regions
	Domain	354 – 584	231	CBM11
	Repeat	530 – 552	23	1
	Repeat	562 – 584	23	2
	Region	25 – 328	304	Catalytic By similarity
	Region	530 – 584	55	2 X 24 AA approximate repeats
	Compositional bias	329 – 353	25	Pro/Thr-rich (linker)
Sites
	Active site	159	1	Proton donor By similarity
	Active site	264	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25472-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 0FC41257E81322C3	FASTA	584	66,062
	10 20 30 40 50 60 MKKILALIIS CSIIMSFLPM SVYGAINSQD MVKKMGIGMN LGNTFDAPTE GSWSKAAQEY 70 80 90 100 110 120 YFDDFKQAGF KHVRIPIRWD QHTLANSPYT VDSNFLNRIE TVIDWSLSRG FVTVINSHHD 130 140 150 160 170 180 TWLMDNYSQN IGRFEKIWEQ IAQRFKGKSE NLVFEILNEP HGNITDSQIN DMNKRILNII 190 200 210 220 230 240 RKTNPTRNVI IGAGYWNSYN SLSQLEIPND PNLIATFHYY DPYSFTHQWQ GTWGTKNDMD 250 260 270 280 290 300 AIAMVFNHVK KWSDKNNIPV YLGEYGVMGH SDRTSAVKWF DFVSDQAISH GFSCGAWDNG 310 320 330 340 350 360 VFGSVDNDMA FYNRDTRQFD KEILNAILTT GTTYDWTPPT ETNPDPPRTP ATPAYGEQLI 370 380 390 400 410 420 EDFEGAMQWA AYSGVDATAS CKISSGKSNN GLEITYAGSS NGYWGVVDNE HRNQDWEKWQ 430 440 450 460 470 480 KISFDIKSSN TNEVRLLIAE QSKIEGEDGE HWTYVIKPST SWTTIEIPFS SFTKRMDYQP 490 500 510 520 530 540 PAQDGSETFD LYKVGSLHFM YSNSNSGTLN IDNIKLIGLP EEQIGGKIGD VNEDGNIDAI 550 560 570 580 DFALLKKYLL DSSISINKVN ADINLDGDIN AIDFAKLKMM LLGD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence analysis of the endoglucanase-encoding gene, celCCD, of Clostridium cellulolyticum." Shima S., Igarashi Y., Kodama T. Gene 104:33-38(1991) [PubMed: 1916275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of Clostridium cellulolyticum H10." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. , Ivanova N., Zhou J., Richardson P. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D90341 Genomic DNA. Translation: BAA14354.1. CP001348 Genomic DNA. Translation: ACL75216.1.
3D structure databases
HSSP	HSSP built from PDB template 1DAV based on UniProtKB P38686.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.2.1.4. 97402.
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. 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. 1 hit.
Pfam	PF03425. CBM_11. 1 hit. PF00150. Cellulase. 1 hit. PF00404. Dockerin_1. 2 hits. [Graphical view]
PROSITE	PS00448. CLOS_CELLULOSOME_RPT. 1 hit. PS00018. EF_HAND_1. 1 hit. Uncertain. PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUND_CLOCE

Accession

Primary (citable) accession number: P25472
Secondary accession number(s): B8I8I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 67 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)