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Protein

Glucan endo-1,3-beta-glucosidase BGN13.1

Gene

bgn13.1

Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in mycoparasitism, hydrolyzes yeast and fungal cell walls. Classified as a small-oligosaccharide-producing type based its the end products: glucose, laminaribiose or laminaritetraose.

Catalytic activityi

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Enzyme regulationi

Inhibited by glucose.

Temperature dependencei

Optimum temperature is 40 degrees Celsius. Inactive at 55 degrees Celsius.

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH55. Glycoside Hydrolase Family 55.
mycoCLAPiLAM55M_TRIHA.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase BGN13.1 (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase BGN13.1
Short name:
(1->3)-beta-glucanase BGN13.1
Basic beta-1,3-endoglucanase BGN13.1
Gene namesi
Name:bgn13.1
OrganismiTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifieri5544 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Propeptidei17 – 3317PRO_0000012227Add
BLAST
Chaini34 – 762729Glucan endo-1,3-beta-glucosidase BGN13.1PRO_0000012228Add
BLAST

Post-translational modificationi

Does not seem to be glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues

Structurei

3D structure databases

ProteinModelPortaliP53626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi520 – 762243Cys-richAdd
BLAST

Domaini

The C-terminal cysteine-rich region may function as a fungal cell wall binding domain.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 55 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 3 hits.

Sequencei

Sequence statusi: Complete.

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

P53626-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKLTALVAL LLGAASATPT PSPPASDEGI TKRATSFYYP NMDHVNAPRG
60 70 80 90 100
FAPDLDGDFN YPIYQTVNAG DGNALQNAIT TDGKGGSRHP QWFASQPRVV
110 120 130 140 150
YIPPGTYTIS KTLRFNTDTI LMGDPTNPPI IKAAAGFSGD QTLISAQDPS
160 170 180 190 200
TNEKGELSFA VAIKNVVLDT TAIPGGNSFT ALWWGVAQAA HLQNVRITMS
210 220 230 240 250
SSSGGNGHTG IRMGRGSTLG LADVRVERGQ NGIWIDGHQQ ASFHNIYFFQ
260 270 280 290 300
NTIGMLISSG NTFSIFSSTF DTCGTAFPTL AGSPWIALID AKSINSGVTF
310 320 330 340 350
TTNQFPSFMI ENLTKDNGTP VVVVRGSTLV GASSHVNTYS YGNTVGRNPT
360 370 380 390 400
YGDVTSSNTR PSALAPGGRY PYVAPPTYGD LPISSFLNVK DPAQNGNRQV
410 420 430 440 450
KGDNTINEAD TLNAILELAA SQNKVAYFPF GKYRVDSTLF IPKGSRIVGE
460 470 480 490 500
AWATITGNGN FFKNENSPQP VVSVGRAGDV GIAQLQDLRV TTNDVLPGAI
510 520 530 540 550
LVQFNMAGNN PGDVALWNSL VTVGGTRGAQ ALANACTNNS NECKGAFIGI
560 570 580 590 600
HVAKGSSPYI QNVWELGLRD HIAENFSGGT SHRRERWNFG PIRRNATCLY
610 620 630 640 650
PIGSGHWWLY QLNLHNAANV VVSLLQAETN YHQGANTQQI PPAPWVANVG
660 670 680 690 700
TWGDPDFSWC NGGDKRCRMG PANFINGGSN IYTYASAAWA FFSGPGQGCA
710 720 730 740 750
QFECQQTIHW IASTPSNLQA FGLCSKDSVN TLRLGDGTFI NTQNGYTGGW
760
TPGGGDVARY TT
Length:762
Mass (Da):81,247
Last modified:October 1, 1996 - v1
Checksum:i0CC25C3C10897AF1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401P → F AA sequence (PubMed:7592488).Curated
Sequence conflicti759 – 7591R → P AA sequence (PubMed:7592488).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84085 mRNA. Translation: CAA58889.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84085 mRNA. Translation: CAA58889.1.

3D structure databases

ProteinModelPortaliP53626.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH55. Glycoside Hydrolase Family 55.
mycoCLAPiLAM55M_TRIHA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 3 hits.
ProtoNetiSearch...

Publicationsi

  1. "A novel endo-beta-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum."
    de la Cruz J., Pintor-Toro J.A., Benitez T., Llobell A., Romero L.C.
    J. Bacteriol. 177:6937-6945(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150.

Entry informationi

Entry nameiE13B_TRIHA
AccessioniPrimary (citable) accession number: P53626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 65 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

Direct protein sequencing

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.