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Q5B7W2 (MANBB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Beta-mannosidase B

EC=3.2.1.25
Alternative name(s):
Mannanase B
Short name=Mannase B
Gene names
Name:mndB
ORF Names:AN3368
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Prefers manobiose over mannotriose and has no activity against polymeric mannan. Is also severly restricetd by galactosyl substitutions at the +1 subsite. Releases the terminal mannose residue from mannobiose, mannotriose and galactosyl-mannotriose (GM3), but not from galactosyl-mannobiose (GM2) or di-galactosyl-mannopentaose (G2M5). Ref.1 Ref.4

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.

Pathway

Glycan metabolism; N-glycan degradation.

Miscellaneous

In contrast to clade A beta-mannosidases, which are likely secreted, clade B proteins appear to be intracellular (Ref.4).

Sequence similarities

Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase B subfamily.

Biophysicochemical properties

Kinetic parameters:

kcat is 79.2 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.

KM=0.22 mM for p-nitrophenyl-beta-mannopyranoside Ref.4

pH dependence:

Optimum pH is 6. Active from pH 5 to 8.

Temperature dependence:

Optimum temperature is 37 degrees Celsius (at pH 6).

Sequence caution

The sequence CBF82847.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA63336.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmannan catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionbeta-mannosidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 843843Beta-mannosidase B
PRO_0000394658

Sites

Active site4321Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5B7W2 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 53B99E1C93DB4055

FASTA84396,367
        10         20         30         40         50         60 
MGAFTQHVLS EGWSFKDSGD QSPDAWLSVP TVPSVVHQDL QANGKLDDPF IGLNELSARW 

        70         80         90        100        110        120 
VNEKSWTYRN VFQKPTVPAG SSIFLVFDGL DTFAKVKLDG QVILESDNMF LAHRVDITKA 

       130        140        150        160        170        180 
LDVEGEHTLE IDFDCALLRA RELRKQHPDH KWVGFNGDTA RLSVRKAQYH WGWDWGPVLM 

       190        200        210        220        230        240 
TAGIWKEVRL EVYSAKISDL WTEVHLAEDH SKARITAAAE VETQGTGNSY KATFTLSLQG 

       250        260        270        280        290        300 
QQIGKEVATL DGNVAKTTFD VQEPSLWWPN GYGDQTLYEI SVSLEKEEEQ AHQVSKKFGI 

       310        320        330        340        350        360 
RTAEVIQRPD KHGKSFFFRI NGVDIFCGGA CWIPADSLLT NITPDRYRKW IELMAVGHQV 

       370        380        390        400        410        420 
MIRVWGGGIY EDESFYQACD EVGVMVWQDF MFGCGNYPTW PEILESIEKE AEYNLRRLRH 

       430        440        450        460        470        480 
HPSIVIWVGN NEDYQVQEQQ GLTYNYADKD PESWLKTDFP ARYIYEHLLP KAVQKIIPSA 

       490        500        510        520        530        540 
YYHPGSPWGD GKITSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI 

       550        560        570        580        590        600 
DHFVTNEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLEVYIYL TQVVQAETMM 

       610        620        630        640        650        660 
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVS RVLKPLAIGV 

       670        680        690        700        710        720 
RREHHDWSVS HAQPPKTSKY ELWVVSSLLK EVIGKVELRF ISIKTGLAIH ESIVRENVTI 

       730        740        750        760        770        780 
VPNGTTNILD GVIDHAVDEP HVLAARLWVD GELVARDVDW PQPFKYLDLS DRGLEITRIS 

       790        800        810        820        830        840 
KTESEQVLEL SARKPVKCLV FEERDNVRVS DSAIDIVPGD EQFVTIKGLK RSDAPLKYKF 


LGQ 

« Hide

References

« Hide 'large scale' references
[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.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
[4]"Phylogenetic analysis and substrate specificity of GH2 beta-mannosidases from Aspergillus species."
Reddy S.K., Rosengren A., Klaubauf S., Kulkarni T., Karlsson E.N., de Vries R.P., Stalbrand H.
FEBS Lett. 587:3444-3449(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490488 mRNA. Translation: ABF50864.1.
AACD01000055 Genomic DNA. Translation: EAA63336.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF82847.1. Sequence problems.
RefSeqXP_660972.1. XM_655880.1.

3D structure databases

ProteinModelPortalQ5B7W2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00009674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00009674; CADANIAP00009674; CADANIAG00009674.
GeneID2874350.
KEGGani:AN3368.2.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000186861.
KOK01192.
OrthoDBEOG7NSB9Q.

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProIPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR028369. Mannanase.
[Graphical view]
PANTHERPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBB_EMENI
AccessionPrimary (citable) accession number: Q5B7W2
Secondary accession number(s): C8VHQ6, Q1HFT6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: May 14, 2014
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries