Exoglucanase B precursor - Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Exoglucanase B
EC=3.2.1.91

Alternative name(s):
1,4-beta-cellobiohydrolase B
CBP120
Exocellobiohydrolase B

Gene names

Name:	cbhB
Synonyms:	cenE
Ordered Locus Names:	Celf_3400

Organism

Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) [Complete proteome] [HAMAP]

Taxonomic identifier

590998 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1090 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

Hydrolyzes cellohexaose to a mixture of cellotetraose, cellotriose and cellobiose, with only a trace of glucose. It hydrolyzed cellopentaose to cellotriose and cellobiose, and cellotetraose to cellobiose, but it did not hydrolyze cellotriose. Has also weak endoglucanase activity. Hydrolyzes glucosidic bonds with inversion of anomeric configuration.

Catalytic activity

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Sequence similarities

Belongs to the glycosyl hydrolase 48 (cellulase L) family.

Contains 1 CBM2 (carbohydrate binding type-2) 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
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cellulose 1,4-beta-cellobiosidase 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

Propeptide

34 – 53

20

PRO_0000008028

Chain

54 – 1090

1037

Exoglucanase B

PRO_0000008029

Regions

Domain

704 – 787

84

Fibronectin type-III 1

Domain

794 – 883

90

Fibronectin type-III 2

Domain

895 – 981

87

Fibronectin type-III 3

Domain

983 – 1090

108

CBM2

Region

54 – 699

646

Catalytic By similarity

Sites

Active site

513

1

Nucleophile By similarity

Amino acid modifications

Disulfide bond

990 ↔ 1089

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P50899 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 046BB9D956F2F399
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FASTA

1,090

114,829

        10         20         30         40         50         60 
MSSTTRRRSA WVAAATVGVS SFLAVAGITP AIAAAGAGQP ATVTVPAASP VRAAVDGEYA 

        70         80         90        100        110        120 
QRFLAQYDKI KDPANGYFSA QGIPYHAVET LMVEAPDYGH ETTSEAYSYW LWLEALYGQV 

       130        140        150        160        170        180 
TQDWAPLNHA WDTMEKYMIP QSVDQPTNSF YNPNSPATYA PEFNHPSSYP SQLNSGISGG 

       190        200        210        220        230        240 
TDPIGAELKA TYGNADVYQM HWLADVDNIY GFGATPGAGC TLGPTATGTS FINTFQRGPQ 

       250        260        270        280        290        300 
ESVWETVPQP SCEEFKYGGK NGYLDLFTKD ASYAKQWKYT SASDADARAV EAVYWANQWA 

       310        320        330        340        350        360 
TEQGKAADVA ATVAKAAKMG DYLRYTLFDK YFKKIGCTSP TCAAGQGREA AHYLLSWYMA 

       370        380        390        400        410        420 
WGGATDTSSG WAWRIGSSHA HFGYQNPLAA WALSTDPKLT PKSPTAKADW AASMQRQLEF 

       430        440        450        460        470        480 
YTWLQASNGG IAGGATNSWD GAYAQPPAGT PTFYGMGYTE APVYVDPPSN RWFGMQAWGV 

       490        500        510        520        530        540 
QRVAELYYAS GNAQAKKILD KWVPWVVANI STDGASWKVP SELKWTGKPD TWNAAAPTGN 

       550        560        570        580        590        600 
PGLTVEVTSY GQDVGVAADT ARALLFYAAK SGDTASRDKA KALLDAIWAN NQDPLGVSAV 

       610        620        630        640        650        660 
ETRGDYKRFD DTYVANGDGI YIPSGWTGTM PNGDVIKPGV SFLDIRSFYK KDPNWSKVQT 

       670        680        690        700        710        720 
FLDGGAEPQF RYHRFWAQTA VAGALADYAR LFDDGTTTPD TTAPTVPTGL QAGVVTSTEA 

       730        740        750        760        770        780 
TISWTASTDD TRVTGYDVYR GATKVGTATT TSFTDTGLTA STAYAYTVRA FDAAGNVSAP 

       790        800        810        820        830        840 
SAALTVTTKA TPSDTTAPSV PAITSSSSTA NSVTIGWSAS TDNAGGSGLA GYDVYRGATR 

       850        860        870        880        890        900 
VAQTTALTFT DTGLTASTAY EYTVRARDVA GNVSAPSTAV SVTTKSDTTP DTTAPSVPAG 

       910        920        930        940        950        960 
LAAMTVTETS VALTWNASTD TGGSGLKGYD VYRGATRVGS TTTASYTDTG LTAATAYQYT 

       970        980        990       1000       1010       1020 
VRATDNAGNV SAASAALSVT TKTPQTGGSC SVAYNASSWN SGFTASVRIT NTGTTTINGW 

      1030       1040       1050       1060       1070       1080 
SLGFDLTAGQ KVQQGWSATW TQSGSTVTAT NAPWNGTLAP GQTVDVGFNG SHTGQNPNPA 

      1090 
SFTLNGASCT

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cellobiohydrolase B, a second exo-cellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi." Shen H., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. Biochem. J. 311:67-74(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 456-461. Strain: ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547.
[2]	"Complete sequence of Cellulomonas fimi ATCC 484." US DOE Joint Genome Institute Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P., Woyke T. Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547.
[3]	"Cellulose-binding polypeptides from Cellulomonas fimi: endoglucanase D (CenD), a family A beta-1,4-glucanase." Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. J. Bacteriol. 175:1910-1918(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-75. Strain: ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547.
[4]	"Stereochemical course of hydrolysis catalysed by Cellulomonas fimi CenE, a member of a new family of beta-1,4-glucanases." Shen H., Tomme P., Meinke A., Gilkes N.R., Kilburn D.G., Warren R.A.J., Miller R.C. Jr. Biochem. Biophys. Res. Commun. 199:1223-1228(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-78.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L38827 Genomic DNA. Translation: AAB00822.1. CP002666 Genomic DNA. Translation: AEE47513.1.
PIR	S59077.
RefSeq	YP_004454900.1. NC_015514.1.
3D structure databases
ProteinModelPortal	P50899.
SMR	P50899. Positions 53-694.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. GH48. Glycoside Hydrolase Family 48.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEE47513; AEE47513; Celf_3400.
GeneID	10594207.
KEGG	cfi:Celf_3400.
PATRIC	54617797. VBICelFim18861_3405.
Organism-specific databases
CMR	Search...
Enzyme and pathway databases
BioCyc	CFIM590998:GJFK-3447-MONOMER.
Family and domain databases
Gene3D	1.50.10.10. 4 hits. 2.60.40.10. 3 hits. 2.60.40.290. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR008965. Carb-bd_dom. IPR012291. CBD_carb-bd_dom. IPR018366. CBM2_CS. IPR001919. Cellulose-bd_dom_fam2_bac. IPR003961. Fibronectin_type3. IPR000556. Glyco_hydro_48F. IPR013783. Ig-like_fold. [Graphical view]
Pfam	PF00553. CBM_2. 1 hit. PF00041. fn3. 3 hits. PF02011. Glyco_hydro_48. 1 hit. [Graphical view]
PRINTS	PR00844. GLHYDRLASE48.
SMART	SM00637. CBD_II. 1 hit. SM00060. FN3. 3 hits. [Graphical view]
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF49265. FN_III-like. 3 hits. SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS50853. FN3. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUXB_CELFA

Accession

Primary (citable) accession number: P50899
Secondary accession number(s): F4H1U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents