Skip Header

Contribute Send feedback
Read comments (?) or add your own

O34559 (URHG2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unsaturated rhamnogalacturonyl hydrolase yteR
Short name=URH
EC=3.2.1.-
Gene names
Name:yteR
Ordered Locus Names:BSU30120
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of unsaturated rhamnogalacturonan disaccharide to yield unsaturated D-galacturonic acid and L-rhamnose. It cannot act on unsaturated glucuronyl hydrolase (UGL) substrates containing unsaturated D-glucuronic acid at the non-reducing terminus, although the active pockets of yesR and UGL are very similar. Ref.3

Subunit structure

Monomer. Ref.3

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 105 family.

Biophysicochemical properties

Kinetic parameters:

KM=100 µM for unsaturated rhamnogalacturonan disaccharide (at pH 4 and 30 degrees Celsius) Ref.3

pH dependence:

Optimum pH is 4.0.

Temperature dependence:

Optimum temperature is 50 degrees Celsius. It is stable below 50 degrees Celsius.

Sequence caution

The sequence CAB14990.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydrolase activity, acting on glycosyl bonds

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 373372Unsaturated rhamnogalacturonyl hydrolase yteR
PRO_0000171597

Regions

Region40 – 412Substrate binding
Region133 – 1364Substrate binding

Sites

Active site1431Proton donor
Binding site3341Substrate
Site411May be essential to modulate pKa of the D-143 carboxyl group
Site881May be essential to modulate pKa of the D-143 carboxyl group

Experimental info

Mutagenesis1431D → N: Loss of hydrolase activity. Ref.3

Secondary structure

1 ..................................................... 373
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34559 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: FC527E1077EB8E86

FASTA37342,969
        10         20         30         40         50         60 
MGSMDQSIAV KSPLTYAEAL ANTIMNTYTV EELPPANRWH YHQGVFLCGV LRLWEATGEK 

        70         80         90        100        110        120 
RYFEYAKAYA DLLIDDNGNL LFRRDELDAI QAGLILFPLY EQTKDERYVK AAKRLRSLYG 

       130        140        150        160        170        180 
TLNRTSEGGF WHKDGYPYQM WLDGLYMGGP FALKYANLKQ ETELFDQVVL QESLMRKHTK 

       190        200        210        220        230        240 
DAKTGLFYHA WDEAKKMPWA NEETGCSPEF WARSIGWYVM SLADMIEELP KKHPNRHVWK 

       250        260        270        280        290        300 
NTLQDMIKSI CRYQDKETGL WYQIVDKGDR SDNWLESSGS CLYMYAIAKG INKGYLDRAY 

       310        320        330        340        350        360 
ETTLLKAYQG LIQHKTETSE DGAFLVKDIC VGTSAGFYDY YVSRERSTND LHGAGAFILA 

       370 
MTELEPLFRS AGK

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"A novel glycoside hydrolase family 105: the structure of family 105 unsaturated rhamnogalacturonyl hydrolase complexed with a disaccharide in comparison with family 88 enzyme complexed with the disaccharide."
Itoh T., Ochiai A., Mikami B., Hashimoto W., Murata K.
J. Mol. Biol. 360:573-585(2006) [PubMed: 16781735] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-6, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF ASP-143, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[4]"1.6 A crystal structure of YteR protein from Bacillus subtilis, a predicted lyase."
Zhang R., Minh T., Lezondra L., Korolev S., Moy S.F., Collart F., Joachimiak A.
Proteins 60:561-565(2005) [PubMed: 15906318] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF008220 Genomic DNA. Translation: AAC00272.1.
AL009126 Genomic DNA. Translation: CAB14990.2. Different initiation.
PIRA69991.
RefSeqNP_390890.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NC5X-ray1.60A1-373[»]
2D8LX-ray1.70A1-373[»]
2GH4X-ray1.90A11-373[»]
ProteinModelPortalO34559.
SMRO34559. Positions 11-373.
ModBaseSearch...

Protein family/group databases

CAZyGH105. Glycoside Hydrolase Family 105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001865; EBBACP00000001865; EBBACG00000001862.
GeneID937273.
GenomeReviewsGene locus BSU30120 in contig AL009126_GR.
KEGGbsu:BSU30120.
NMPDRfig|224308.1.peg.3015.
PATRIC18977928. VBIBacSub10457_3152.

Organism-specific databases

GenoListBSU30120.

Phylogenomic databases

GeneTreeEBGT00050000006136.
HOGENOMHBG301559.
OMAHYHQGVF.
PhylomeDBO34559.
ProtClustDBCLSK872720.

Enzyme and pathway databases

BioCycBSUB:BSU30120-MONOMER.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR010905. Glyco_hydro_88.
[Graphical view]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
KOK15532.
PfamPF07470. Glyco_hydro_88. 1 hit.
[Graphical view]
SUPFAMSSF48208. Glyco_trans_6hp. 1 hit.
ProtoNetSearch...

Entry information

Entry nameURHG2_BACSU
AccessionPrimary (citable) accession number: O34559
Secondary accession number(s): Q795R4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents