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Q5B7W2

- MANBB_EMENI

UniProt

Q5B7W2 - MANBB_EMENI

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Protein
Beta-mannosidase B
Gene
mndB, AN3368
Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - 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.

Temperature dependencei

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei432 – 4321Proton donor By 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: Chromosome VI

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843Beta-mannosidase B
PRO_0000394658Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00009674.

Structurei

3D structure databases

ProteinModelPortaliQ5B7W2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
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

MGAFTQHVLS EGWSFKDSGD QSPDAWLSVP TVPSVVHQDL QANGKLDDPF    50
IGLNELSARW VNEKSWTYRN VFQKPTVPAG SSIFLVFDGL DTFAKVKLDG 100
QVILESDNMF LAHRVDITKA LDVEGEHTLE IDFDCALLRA RELRKQHPDH 150
KWVGFNGDTA RLSVRKAQYH WGWDWGPVLM TAGIWKEVRL EVYSAKISDL 200
WTEVHLAEDH SKARITAAAE VETQGTGNSY KATFTLSLQG QQIGKEVATL 250
DGNVAKTTFD VQEPSLWWPN GYGDQTLYEI SVSLEKEEEQ AHQVSKKFGI 300
RTAEVIQRPD KHGKSFFFRI NGVDIFCGGA CWIPADSLLT NITPDRYRKW 350
IELMAVGHQV MIRVWGGGIY EDESFYQACD EVGVMVWQDF MFGCGNYPTW 400
PEILESIEKE AEYNLRRLRH HPSIVIWVGN NEDYQVQEQQ GLTYNYADKD 450
PESWLKTDFP ARYIYEHLLP KAVQKIIPSA YYHPGSPWGD GKITSDPTVG 500
DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI DHFVTNEADK 550
YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLEVYIYL TQVVQAETMM 600
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVS 650
RVLKPLAIGV RREHHDWSVS HAQPPKTSKY ELWVVSSLLK EVIGKVELRF 700
ISIKTGLAIH ESIVRENVTI VPNGTTNILD GVIDHAVDEP HVLAARLWVD 750
GELVARDVDW PQPFKYLDLS DRGLEITRIS KTESEQVLEL SARKPVKCLV 800
FEERDNVRVS DSAIDIVPGD EQFVTIKGLK RSDAPLKYKF LGQ 843
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.
The sequence EAA63336.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DQ490488 mRNA. Translation: ABF50864.1 .
AACD01000055 Genomic DNA. Translation: EAA63336.1 . Sequence problems.
BN001306 Genomic DNA. Translation: CBF82847.1 . Sequence problems.
RefSeqi XP_660972.1. XM_655880.1.

3D structure databases

ProteinModelPortali Q5B7W2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00009674.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00009674 ; CADANIAP00009674 ; CADANIAG00009674 .
GeneIDi 2874350.
KEGGi ani:AN3368.2.

Phylogenomic databases

eggNOGi COG3250.
HOGENOMi HOG000186861.
KOi K01192.
OrthoDBi EOG7NSB9Q.

Enzyme and pathway databases

UniPathwayi UPA00280 .

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR008979. 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 ]
PANTHERi PTHR10066:SF12. PTHR10066:SF12. 1 hit.
Pfami PF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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: May 14, 2014
This is version 64 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

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