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Protein

Beta-mannosidase B

Gene

mndB

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

Functioni

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).2 Publications

Catalytic activityi

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

Kineticsi

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

  1. KM=0.22 mM for p-nitrophenyl-beta-mannopyranoside1 Publication

pH dependencei

Optimum pH is 6. Active from pH 5 to 8.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius (at pH 6).1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei432 – 4321Proton donorBy similarity

GO - Molecular functioni

  1. beta-mannosidase activity Source: UniProtKB

GO - Biological processi

  1. mannan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00280.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-mannosidase B (EC:3.2.1.25)
Alternative name(s):
Mannanase B
Short name:
Mannase B
Gene namesi
Name:mndB
ORF Names:AN3368
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VI

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843Beta-mannosidase BPRO_0000394658Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00009674.

Structurei

3D structure databases

ProteinModelPortaliQ5B7W2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
InParanoidiQ5B7W2.
KOiK01192.
OrthoDBiEOG7NSB9Q.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008979. 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]
PANTHERiPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamiPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5B7W2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAFTQHVLS EGWSFKDSGD QSPDAWLSVP TVPSVVHQDL QANGKLDDPF
60 70 80 90 100
IGLNELSARW VNEKSWTYRN VFQKPTVPAG SSIFLVFDGL DTFAKVKLDG
110 120 130 140 150
QVILESDNMF LAHRVDITKA LDVEGEHTLE IDFDCALLRA RELRKQHPDH
160 170 180 190 200
KWVGFNGDTA RLSVRKAQYH WGWDWGPVLM TAGIWKEVRL EVYSAKISDL
210 220 230 240 250
WTEVHLAEDH SKARITAAAE VETQGTGNSY KATFTLSLQG QQIGKEVATL
260 270 280 290 300
DGNVAKTTFD VQEPSLWWPN GYGDQTLYEI SVSLEKEEEQ AHQVSKKFGI
310 320 330 340 350
RTAEVIQRPD KHGKSFFFRI NGVDIFCGGA CWIPADSLLT NITPDRYRKW
360 370 380 390 400
IELMAVGHQV MIRVWGGGIY EDESFYQACD EVGVMVWQDF MFGCGNYPTW
410 420 430 440 450
PEILESIEKE AEYNLRRLRH HPSIVIWVGN NEDYQVQEQQ GLTYNYADKD
460 470 480 490 500
PESWLKTDFP ARYIYEHLLP KAVQKIIPSA YYHPGSPWGD GKITSDPTVG
510 520 530 540 550
DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI DHFVTNEADK
560 570 580 590 600
YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLEVYIYL TQVVQAETMM
610 620 630 640 650
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVS
660 670 680 690 700
RVLKPLAIGV RREHHDWSVS HAQPPKTSKY ELWVVSSLLK EVIGKVELRF
710 720 730 740 750
ISIKTGLAIH ESIVRENVTI VPNGTTNILD GVIDHAVDEP HVLAARLWVD
760 770 780 790 800
GELVARDVDW PQPFKYLDLS DRGLEITRIS KTESEQVLEL SARKPVKCLV
810 820 830 840
FEERDNVRVS DSAIDIVPGD EQFVTIKGLK RSDAPLKYKF LGQ
Length:843
Mass (Da):96,367
Last modified:June 15, 2010 - v2
Checksum:i53B99E1C93DB4055
GO

Sequence cautioni

The sequence CBF82847.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA63336.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490488 mRNA. Translation: ABF50864.1.
AACD01000055 Genomic DNA. Translation: EAA63336.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF82847.1. Sequence problems.
RefSeqiXP_660972.1. XM_655880.1.

Genome annotation databases

EnsemblFungiiCADANIAT00009674; CADANIAP00009674; CADANIAG00009674.
GeneIDi2874350.
KEGGiani:AN3368.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490488 mRNA. Translation: ABF50864.1.
AACD01000055 Genomic DNA. Translation: EAA63336.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF82847.1. Sequence problems.
RefSeqiXP_660972.1. XM_655880.1.

3D structure databases

ProteinModelPortaliQ5B7W2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00009674.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00009674; CADANIAP00009674; CADANIAG00009674.
GeneIDi2874350.
KEGGiani:AN3368.2.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
InParanoidiQ5B7W2.
KOiK01192.
OrthoDBiEOG7NSB9Q.

Enzyme and pathway databases

UniPathwayiUPA00280.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008979. 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]
PANTHERiPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamiPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

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.
    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.
  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.

Entry informationi

Entry nameiMANBB_EMENI
AccessioniPrimary (citable) accession number: Q5B7W2
Secondary accession number(s): C8VHQ6, Q1HFT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: February 4, 2015
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to clade A beta-mannosidases, which are likely secreted, clade B proteins appear to be intracellular.1 Publication

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

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.