P26225 (GUNB_CELFI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase B
EC=3.2.1.4

Alternative name(s):
Cellulase B
Endo-1,4-beta-glucanase B

Gene names

Name:

cenB

Organism

Cellulomonas fimi

Taxonomic identifier

1708 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	1045 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.
Domain	The linker region (also termed "hinge") may be a potential site for proteolysis. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 9 (cellulase E) family. Contains 1 CBM2 (carbohydrate binding type-2) domain. Contains 1 CBM3 (carbohydrate binding type-3) domain. Contains 3 fibronectin type-III domains.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cellulase activity Inferred from electronic annotation. Source: EC polysaccharide binding 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 – 33	33	Potential
	Chain	34 – 1045	1012	Endoglucanase B		PRO_0000007945
Regions
	Domain	493 – 642	150	CBM3
	Domain	650 – 740	91	Fibronectin type-III 1
	Domain	748 – 837	90	Fibronectin type-III 2
	Domain	847 – 937	91	Fibronectin type-III 3
	Domain	939 – 1045	107	CBM2
	Region	34 – 492	459	Catalytic
	Region	644 – 650	7	Linker ("hinge") (Pro-Thr box)
	Region	734 – 748	15	Linker ("hinge") (Pro-Thr box)
	Region	831 – 846	16	Linker ("hinge") (Pro-Thr box)
	Region	931 – 944	14	Linker ("hinge") (Pro-Thr box)
Sites
	Active site	410	1	By similarity
	Active site	449	1	By similarity
	Active site	458	1	By similarity
Amino acid modifications
	Disulfide bond	946 ↔ 1044		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26225 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: AC2F7B84E4E3C4F0	FASTA	1,045	108,991
	10 20 30 40 50 60 MLRQVPRTLV AGGSALAVAV GVLVAPLATG AAAAPTYNYA EALQKSMFFY QAQRSGDLPA 70 80 90 100 110 120 DFPVSWRGDS GLTDGADVGK DLTGGWYDAG DHVKFGFPMA FSATMLAWGA IESPTGYSKA 130 140 150 160 170 180 GSLDELKDNL RFVSDYFVKA HTAPNELYVQ VGDGEADHKW WGPAEVMTMA RPSHKISASC 190 200 210 220 230 240 PGSDVAAETA AALASSAIVL KGDDPAYAAT LVSHAKQLYT FADTYRGAYS DCVTAASAYY 250 260 270 280 290 300 KSWSGYQDEL VWGAYWLYKA TGDATYLAKA EAEYDKLGTE NQSTTRSYKW TIAWDNKQFG 310 320 330 340 350 360 TYALLAMETG KQKYVDDANR WLDYWTVGVN GQKVPYSPGG QAVLDSWGAL RYAANTSFVA 370 380 390 400 410 420 LVYSDWMTDA TRKARYHDFG VRQINYALGD NPRSSSYVVG FGANPPTAPH HRTAHGSWLD 430 440 450 460 470 480 SITTPAQSRH VLYGALVGGP GSPNDAYTDS RQDYVANEVA TDYNAGFTSA LARLVEEYGG 490 500 510 520 530 540 TPLASFPTPE QPDGDQLFVE AMLNQPPSGT FTEVKAMIRN QSAFPARSLK NAKVRYWFTT 550 560 570 580 590 600 DGFAASDVTL SANYSECGAQ SGKGVSAGGT LGYVELSCVG QDIHPGGQSQ HRREIQFRLT 610 620 630 640 650 660 GPAGWNPAND PSYTGLTQTA LAKASAITLY DGSTLVWGKE PTGTTTDTTP PTTPGTPVAT 670 680 690 700 710 720 GVTTVGASLS WAASTDAGSG VAGYELYRVQ GTTQTLVGTT TAAAYILRDL TPGTAYSYVV 730 740 750 760 770 780 KAKDVAGNVS AASAAVTFTT DTTGETEPPT TPGTPVASAV TSTGATLAWA PSTGDPAVSG 790 800 810 820 830 840 YDVLRVQGTT TTVVAQTTVP TVTLSGLTPS TAYTYAVRAK NVAGDVSALS APVTFTTAAP 850 860 870 880 890 900 PVDTVAPTVP GTPVASNVAT TGATLTWTAS TDSGGSGLAG YEVLRVSGTT QTLVASPTTA 910 920 930 940 950 960 TVALAGLTPA TAYSYVVRAK DGAGNVSAVS SPVTFTTLPV TSTPSCTVVY STNSWNVGFT 970 980 990 1000 1010 1020 GSVKITNTGT TPLTWTLGFA FPSGQQVTQG WSATWSQTGT TVTATGLSWN ATLQPGQSTD 1030 1040 IGFNGSHPGT NTNPASFTVN GEVCG

References

[1]	"Unusual sequence organization in CenB, an inverting endoglucanase from Cellulomonas fimi." Meinke A., Braun C., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. J. Bacteriol. 173:308-314(1991) [PubMed: 1987122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Multiple domains in endoglucanase B (CenB) from Cellulomonas fimi: functions and relatedness to domains in other polypeptides." Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. J. Bacteriol. 173:7126-7135(1991) [PubMed: 1938913] [Abstract] Cited for: DOMAINS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64644 Genomic DNA. Translation: AAA23086.1.
PIR	A39199.
3D structure databases
ProteinModelPortal	P26225.
SMR	P26225. Positions 35-641.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. CBM3. Carbohydrate-Binding Module Family 3. GH9. Glycoside Hydrolase Family 9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR008965. Carb-bd_dom. IPR001956. CBD_3. IPR012291. CBD_carb-bd_dom. IPR018366. CBM2_CS. IPR001919. Cellulose-bd_dom_fam2_bac. IPR003961. Fibronectin_type3. IPR001701. Glyco_hydro_9. IPR018221. Glyco_hydro_9_AS. IPR013783. Ig-like_fold. [Graphical view]
Gene3D	G3DSA:2.60.40.710. CBD_3. 1 hit. G3DSA:2.60.40.290. CBD_carb_bd. 1 hit. G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 3 hits.
Pfam	PF00553. CBM_2. 1 hit. PF00942. CBM_3. 1 hit. PF00041. fn3. 3 hits. PF00759. Glyco_hydro_9. 1 hit. [Graphical view]
SMART	SM00637. CBD_II. 1 hit. SM01067. CBM_3. 1 hit. SM00060. FN3. 3 hits. [Graphical view]
SUPFAM	SSF49384. Cellul_bind. 2 hits. SSF49265. FN_III-like. 3 hits. SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS51172. CBM3. 1 hit. PS50853. FN3. 3 hits. PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit. PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNB_CELFI

Accession

Primary (citable) accession number: P26225

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program