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Q5BFG8

- BGLB_EMENI

UniProt

Q5BFG8 - BGLB_EMENI

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Protein

Beta-glucosidase B

Gene

bglB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

pH dependencei

Optimum pH is 5.5.1 Publication

Temperature dependencei

Optimum temperature is 52 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei230 – 2301By similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
  2. glucan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase B (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase B
Cellobiase B
Gentiobiase B
Gene namesi
Name:bglB
ORF Names:AN0712
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VIII

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 845845Beta-glucosidase BPRO_0000394102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi794 – 7941N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5BFG8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000031215.
InParanoidiQ5BFG8.
KOiK05349.
OMAiANEQETE.
OrthoDBiEOG7H799Q.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 3 hits.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 3 hits.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5BFG8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFQKVDPAQ IESVLSKLTL EEKISLLAGK NFWETQDYPE KGVPPVKTSD
60 70 80 90 100
GPNGARGATF KGGVTAACFP ASSLLAATWD LDAAKHIGEA LADETRSKGA
110 120 130 140 150
RVLLAPTVCI HRHPLGGRNF ESFSEDPFLA GKLAAQYIKG LQGNGVAATI
160 170 180 190 200
KHYAANEQET CRFTVNEHIT ERALREIYLK PFEIAIKESN PLAVMTAYNI
210 220 230 240 250
VNGTHADSNN FLLRDVLRGE WGWKGLVMSD WGGTNSTADA LNAGLDLEMP
260 270 280 290 300
GPTRWRKVDE VLAVVKSGAV LEETIDERAR NVLELLAKLN CFENPTIPEE
310 320 330 340 350
KAINRPEHQK LIRSVGSQGL VLLKNEGDVL PLRKEILTNK KVALLGFARE
360 370 380 390 400
ALIHGGGSAS VNAHYRVTPE EGLRAALGDT VEFEYAKGAH TFRQLPLMSD
410 420 430 440 450
NVVNLEGQPG WTLDFFADEE PNGEPGSSIS SEQPSYIPLF VKESWGSVRA
460 470 480 490 500
SAHFTPTQSG KHYFGMSGLG RSKLLIDGEV IYEQKLNCPD SMGFLLGGVE
510 520 530 540 550
EPEIQYSFEA GKTYAVEVVS VKPTSKGGLA LLDGFIGFRL GFMTEEEHNR
560 570 580 590 600
DLLSEAVDVA KRSDIAIVFT GHTPDWETEG QDQISFHLPS NGSQDRLVAA
610 620 630 640 650
VGAANPNTVV VNCTGVAVAM PWLDKVKAVV QAWFPGQEAG NAIADVLTGA
660 670 680 690 700
VNPSGRLPVS FPRAIEDAPA HGNFPGDYTD GKDNRRHLEV TYKEGVFVGY
710 720 730 740 750
RHYDLSEANR AKVLFPFGYG LSYTTFTHAN HKASATSRNT VEVAVDVTNV
760 770 780 790 800
GTCAGADVVQ VYAGAKLAVP ENPVKELVGF AKVHLKPGET KTANITFEVR
810 820 830 840
QLTHFTERSG KWELESGDYE ISIGQSVRDI TGKVEIGLEA QNYKP
Length:845
Mass (Da):91,790
Last modified:April 26, 2005 - v1
Checksum:iAEB0E7A749BC0C25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490467 mRNA. Translation: ABF50843.1.
AACD01000011 Genomic DNA. Translation: EAA65189.1.
BN001308 Genomic DNA. Translation: CBF88936.1.
RefSeqiXP_658316.1. XM_653224.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001957; CADANIAP00001957; CADANIAG00001957.
GeneIDi2876490.
KEGGiani:AN0712.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490467 mRNA. Translation: ABF50843.1 .
AACD01000011 Genomic DNA. Translation: EAA65189.1 .
BN001308 Genomic DNA. Translation: CBF88936.1 .
RefSeqi XP_658316.1. XM_653224.1.

3D structure databases

ProteinModelPortali Q5BFG8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00001957 ; CADANIAP00001957 ; CADANIAG00001957 .
GeneIDi 2876490.
KEGGi ani:AN0712.2.

Phylogenomic databases

eggNOGi COG1472.
HOGENOMi HOG000031215.
InParanoidi Q5BFG8.
KOi K05349.
OMAi ANEQETE.
OrthoDBi EOG7H799Q.

Enzyme and pathway databases

UniPathwayi UPA00696 .

Family and domain databases

Gene3Di 3.20.20.300. 1 hit.
3.40.50.1700. 3 hits.
InterProi IPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR30620. PTHR30620. 1 hit.
Pfami PF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view ]
PRINTSi PR00133. GLHYDRLASE3.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 3 hits.
PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiBGLB_EMENI
AccessioniPrimary (citable) accession number: Q5BFG8
Secondary accession number(s): C8VRC8, Q1HFV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 57 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

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3