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Q00019 (RHGB_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Rhamnogalacturonase B
EC=4.2.2.-
Alternative name(s):
RGase B
RHG B
Rhamnogalacturonan lyase
Gene names
Name:rhgB
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pectinolytic enzyme that has a positive effect in the apple hot-mash liquefaction process. This endolyase hydrolyzes the alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage by beta-elimination, thereby generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.

Sequence similarities

Belongs to the polysaccharide lyase 4 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0, enzymatic activity becomes unstable below this value.

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Ontologies

Keywords
   DomainSignal
   Molecular functionLyase
   PTMGlycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

carbon-oxygen lyase activity, acting on polysaccharides

Inferred from electronic annotation. Source: InterPro

carboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 527508Rhamnogalacturonase B
PRO_0000024912

Amino acid modifications

Glycosylation3501N-linked (GlcNAc...) Potential

Secondary structure

1 ................................................................................................. 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00019 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B0E14412E5CDC080

FASTA52756,190
        10         20         30         40         50         60 
MLKASLLSFV AFTAQVAHAA FGITTSSSAY VIDTNAPNQL KFTVSRSSCD ITSIIHYGTE 

        70         80         90        100        110        120 
LQYSSQGSHI GSGLGSATVT ATQSGDYIKV TCVTDTLTQY MVVHNGDPII HMATYITAEP 

       130        140        150        160        170        180 
SIGELRFIAR LNSDLLPNEE PFGDVSTTAD GTAIEGSDVF LVGSETRSKF YSSERFIDDQ 

       190        200        210        220        230        240 
RHCIAGDAHR VCMILNQYES SSGGPFHRDI NSNNGGSYNA LYWYMNSGHV QTESYRMGLH 

       250        260        270        280        290        300 
GPYSMYFSRS GTPSTSIDTS FFADLDIKGY VAASGRGKVA GTASGADSSM DWVVHWYNDA 

       310        320        330        340        350        360 
AQYWTYTSSS GSFTSPAMKP GTYTMVYYQG EYAVATSSVT VSAGSTTTKN ISGSVKTGTT 

       370        380        390        400        410        420 
IFKIGEWDGQ PTGFRNAANQ LRMHPSDSRM SSWGPLTYTV GSSALTDFPM AVFKSVNNPV 

       430        440        450        460        470        480 
TIKFTATSAQ TGAATLRIGT TLSFAGGRPQ ATINSYTGSA PAAPTNLDSR GVTRGAYRGL 

       490        500        510        520 
GEVYDVSIPS GTIVAGTNTI TINVISGSSG DTYLSPNFIF DCVELFQ

« Hide

References

[1]"Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus."
Kofod L.V., Kauppinen S., Christgau S., Andersen L.N., Heldt-Hansen H.P., Doerreich K., Dalboege H.
J. Biol. Chem. 269:29182-29189(1994) [PubMed: 7961884] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: KSM 510.
[2]"The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase."
Azadi P., O'Neill M.A., Bergmann C., Darvill A.G., Albersheim P.
Glycobiology 5:783-789(1995) [PubMed: 8720076] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L35500 mRNA. Translation: AAA64368.1.
PIRB55415.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKGX-ray1.50A20-527[»]
2XHNX-ray1.52A/B20-527[»]
3NJVX-ray2.40A20-527[»]
3NJXX-ray1.94A20-527[»]
ProteinModelPortalQ00019.
SMRQ00019. Positions 20-527.
ModBaseSearch...

Protein family/group databases

CAZyPL4. Polysaccharide Lyase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16403.

Family and domain databases

InterProIPR013784. Carb-bd-like_fold.
IPR014766. CarboxyPept_regulatory_dom.
IPR008979. Galactose-bd-like.
IPR011013. Glyco_hydro-type_carb-bd.
IPR016590. Rhamnogalacturonase_B.
IPR015364. RhgB_N.
[Graphical view]
Gene3DG3DSA:2.60.40.1120. CarboxyPept_regulatory. 1 hit.
PfamPF09284. RhgB_N. 1 hit.
[Graphical view]
PIRSFPIRSF011794. Rhamnogalacturonase_B. 1 hit.
SUPFAMSSF49452. CBD_4. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF74650. Gal_mut_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRHGB_ASPAC
AccessionPrimary (citable) accession number: Q00019
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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