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Protein

Exoglucanase B

Gene

cbhB

Organism
Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei513 – 5131NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: InterPro
  2. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
  3. polysaccharide binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCFIM590998:GJFK-3447-MONOMER.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH48. Glycoside Hydrolase Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase B (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase B
CBP120
Exocellobiohydrolase B
Gene namesi
Name:cbhB
Synonyms:cenE
Ordered Locus Names:Celf_3400
OrganismiCellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547)
Taxonomic identifieri590998 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas
ProteomesiUP000008460 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Propeptidei34 – 53202 PublicationsPRO_0000008028Add
BLAST
Chaini54 – 10901037Exoglucanase BPRO_0000008029Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi990 ↔ 1089By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP50899.
SMRiP50899. Positions 53-694.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini706 – 79186Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini797 – 88791Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini897 – 98488Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini983 – 1090108CBM2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 699646CatalyticBy similarityAdd
BLAST

Sequence similaritiesi

Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

OMAiWLWLEAL.

Family and domain databases

Gene3Di1.50.10.10. 4 hits.
2.60.40.10. 3 hits.
2.60.40.290. 1 hit.
4.10.870.10. 1 hit.
InterProiIPR008928. 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.
IPR027390. Endoglucanase_F_dom3.
IPR003961. FN3_dom.
IPR000556. Glyco_hydro_48F.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00041. fn3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SMARTiSM00637. CBD_II. 1 hit.
SM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 2 hits.
SSF49384. SSF49384. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS50853. FN3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P50899-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTTRRRSA WVAAATVGVS SFLAVAGITP AIAAAGAGQP ATVTVPAASP
60 70 80 90 100
VRAAVDGEYA QRFLAQYDKI KDPANGYFSA QGIPYHAVET LMVEAPDYGH
110 120 130 140 150
ETTSEAYSYW LWLEALYGQV TQDWAPLNHA WDTMEKYMIP QSVDQPTNSF
160 170 180 190 200
YNPNSPATYA PEFNHPSSYP SQLNSGISGG TDPIGAELKA TYGNADVYQM
210 220 230 240 250
HWLADVDNIY GFGATPGAGC TLGPTATGTS FINTFQRGPQ ESVWETVPQP
260 270 280 290 300
SCEEFKYGGK NGYLDLFTKD ASYAKQWKYT SASDADARAV EAVYWANQWA
310 320 330 340 350
TEQGKAADVA ATVAKAAKMG DYLRYTLFDK YFKKIGCTSP TCAAGQGREA
360 370 380 390 400
AHYLLSWYMA WGGATDTSSG WAWRIGSSHA HFGYQNPLAA WALSTDPKLT
410 420 430 440 450
PKSPTAKADW AASMQRQLEF YTWLQASNGG IAGGATNSWD GAYAQPPAGT
460 470 480 490 500
PTFYGMGYTE APVYVDPPSN RWFGMQAWGV QRVAELYYAS GNAQAKKILD
510 520 530 540 550
KWVPWVVANI STDGASWKVP SELKWTGKPD TWNAAAPTGN PGLTVEVTSY
560 570 580 590 600
GQDVGVAADT ARALLFYAAK SGDTASRDKA KALLDAIWAN NQDPLGVSAV
610 620 630 640 650
ETRGDYKRFD DTYVANGDGI YIPSGWTGTM PNGDVIKPGV SFLDIRSFYK
660 670 680 690 700
KDPNWSKVQT FLDGGAEPQF RYHRFWAQTA VAGALADYAR LFDDGTTTPD
710 720 730 740 750
TTAPTVPTGL QAGVVTSTEA TISWTASTDD TRVTGYDVYR GATKVGTATT
760 770 780 790 800
TSFTDTGLTA STAYAYTVRA FDAAGNVSAP SAALTVTTKA TPSDTTAPSV
810 820 830 840 850
PAITSSSSTA NSVTIGWSAS TDNAGGSGLA GYDVYRGATR VAQTTALTFT
860 870 880 890 900
DTGLTASTAY EYTVRARDVA GNVSAPSTAV SVTTKSDTTP DTTAPSVPAG
910 920 930 940 950
LAAMTVTETS VALTWNASTD TGGSGLKGYD VYRGATRVGS TTTASYTDTG
960 970 980 990 1000
LTAATAYQYT VRATDNAGNV SAASAALSVT TKTPQTGGSC SVAYNASSWN
1010 1020 1030 1040 1050
SGFTASVRIT NTGTTTINGW SLGFDLTAGQ KVQQGWSATW TQSGSTVTAT
1060 1070 1080 1090
NAPWNGTLAP GQTVDVGFNG SHTGQNPNPA SFTLNGASCT
Length:1,090
Mass (Da):114,829
Last modified:September 30, 1996 - v1
Checksum:i046BB9D956F2F399
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38827 Genomic DNA. Translation: AAB00822.1.
CP002666 Genomic DNA. Translation: AEE47513.1.
PIRiS59077.
RefSeqiWP_013772537.1. NC_015514.1.
YP_004454900.1. NC_015514.1.

Genome annotation databases

EnsemblBacteriaiAEE47513; AEE47513; Celf_3400.
KEGGicfi:Celf_3400.
PATRICi54617797. VBICelFim18861_3405.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38827 Genomic DNA. Translation: AAB00822.1.
CP002666 Genomic DNA. Translation: AEE47513.1.
PIRiS59077.
RefSeqiWP_013772537.1. NC_015514.1.
YP_004454900.1. NC_015514.1.

3D structure databases

ProteinModelPortaliP50899.
SMRiP50899. Positions 53-694.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEE47513; AEE47513; Celf_3400.
KEGGicfi:Celf_3400.
PATRICi54617797. VBICelFim18861_3405.

Phylogenomic databases

OMAiWLWLEAL.

Enzyme and pathway databases

BioCyciCFIM590998:GJFK-3447-MONOMER.

Family and domain databases

Gene3Di1.50.10.10. 4 hits.
2.60.40.10. 3 hits.
2.60.40.290. 1 hit.
4.10.870.10. 1 hit.
InterProiIPR008928. 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.
IPR027390. Endoglucanase_F_dom3.
IPR003961. FN3_dom.
IPR000556. Glyco_hydro_48F.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00041. fn3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SMARTiSM00637. CBD_II. 1 hit.
SM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 2 hits.
SSF49384. SSF49384. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS50853. FN3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [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 (MAR-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(1992) [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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-78.

Entry informationi

Entry nameiGUXB_CELFA
AccessioniPrimary (citable) accession number: P50899
Secondary accession number(s): F4H1U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: March 31, 2015
This is version 86 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.