Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable 1,4-beta-D-glucan cellobiohydrolase B

Gene

cbhB

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

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 sitei238 – 2381NucleophileBy similarity
Active sitei243 – 2431Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 1,4-beta-D-glucan cellobiohydrolase B (EC:3.2.1.91)
Alternative name(s):
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B
Gene namesi
Name:cbhB
ORF Names:AFUA_6G11610
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiFungiDB:Afu6g11610.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 532506Probable 1,4-beta-D-glucan cellobiohydrolase BPRO_0000393548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi504 ↔ 521By similarity
Disulfide bondi515 ↔ 531By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

Expressed at high levels in the presence of carboxymethylcellulose and repressed in the presence of glucose.1 Publication

Structurei

Secondary structure

1
532
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 454Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 604Combined sources
Helixi62 – 643Combined sources
Beta strandi67 – 693Combined sources
Beta strandi75 – 784Combined sources
Turni84 – 863Combined sources
Helixi90 – 967Combined sources
Beta strandi97 – 993Combined sources
Helixi104 – 1085Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi116 – 13015Combined sources
Beta strandi132 – 1398Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi166 – 1738Combined sources
Turni177 – 1837Combined sources
Helixi190 – 1934Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi238 – 2447Combined sources
Beta strandi249 – 2546Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi262 – 2654Combined sources
Helixi266 – 2694Combined sources
Beta strandi279 – 2824Combined sources
Turni291 – 2955Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi312 – 3209Combined sources
Beta strandi329 – 33810Combined sources
Beta strandi341 – 3444Combined sources
Beta strandi356 – 3583Combined sources
Helixi360 – 37011Combined sources
Helixi375 – 3784Combined sources
Helixi381 – 39111Combined sources
Beta strandi393 – 4019Combined sources
Turni403 – 4075Combined sources
Helixi408 – 4114Combined sources
Beta strandi412 – 4154Combined sources
Turni423 – 4253Combined sources
Helixi437 – 4437Combined sources
Beta strandi448 – 45811Combined sources
Turni459 – 4646Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V1ZX-ray1.78A28-466[»]
4V20X-ray1.50A28-466[»]
ProteinModelPortaliQ4WM08.
SMRiQ4WM08. Positions 27-463, 500-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini496 – 53237CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 461435CatalyticAdd
BLAST
Regioni462 – 49635Thr-rich linkerAdd
BLAST

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000182210.
InParanoidiQ4WM08.
KOiK01238.
OMAiRGSCDIS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q4WM08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLASTFSYRM YKTALILAAL LGSGQAQQVG TSQAEVHPSM TWQSCTAGGS
60 70 80 90 100
CTTNNGKVVI DANWRWVHKV GDYTNCYTGN TWDTTICPDD ATCASNCALE
110 120 130 140 150
GANYESTYGV TASGNSLRLN FVTTSQQKNI GSRLYMMKDD STYEMFKLLN
160 170 180 190 200
QEFTFDVDVS NLPCGLNGAL YFVAMDADGG MSKYPTNKAG AKYGTGYCDS
210 220 230 240 250
QCPRDLKFIN GQANVEGWQP SSNDANAGTG NHGSCCAEMD IWEANSISTA
260 270 280 290 300
FTPHPCDTPG QVMCTGDACG GTYSSDRYGG TCDPDGCDFN SFRQGNKTFY
310 320 330 340 350
GPGMTVDTKS KFTVVTQFIT DDGTSSGTLK EIKRFYVQNG KVIPNSESTW
360 370 380 390 400
TGVSGNSITT EYCTAQKSLF QDQNVFEKHG GLEGMGAALA QGMVLVMSLW
410 420 430 440 450
DDHSANMLWL DSNYPTTASS TTPGVARGTC DISSGVPADV EANHPDAYVV
460 470 480 490 500
YSNIKVGPIG STFNSGGSNP GGGTTTTTTT QPTTTTTTAG NPGGTGVAQH
510 520 530
YGQCGGIGWT GPTTCASPYT CQKLNDYYSQ CL
Length:532
Mass (Da):56,457
Last modified:July 5, 2005 - v1
Checksum:i03EBC7D15A5EAE78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL89006.1.
RefSeqiXP_751044.1. XM_745951.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00002184; CADAFUAP00002184; CADAFUAG00002184.
GeneIDi3508349.
KEGGiafm:AFUA_6G11610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL89006.1.
RefSeqiXP_751044.1. XM_745951.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V1ZX-ray1.78A28-466[»]
4V20X-ray1.50A28-466[»]
ProteinModelPortaliQ4WM08.
SMRiQ4WM08. Positions 27-463, 500-532.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00002184; CADAFUAP00002184; CADAFUAG00002184.
GeneIDi3508349.
KEGGiafm:AFUA_6G11610.

Organism-specific databases

EuPathDBiFungiDB:Afu6g11610.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000182210.
InParanoidiQ4WM08.
KOiK01238.
OMAiRGSCDIS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
  2. "The Aspergillus fumigatus cellobiohydrolase B (cbhB) promoter is tightly regulated and can be exploited for controlled protein expression and RNAi."
    Bromley M., Gordon C., Rovira-Graells N., Oliver J.
    FEMS Microbiol. Lett. 264:246-254(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiCBHB_ASPFU
AccessioniPrimary (citable) accession number: Q4WM08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: July 5, 2005
Last modified: June 24, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.