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Protein

Mannan endo-1,4-beta-mannosidase B

Gene

manB

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 transcript leveli

Functioni

Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar.1 Publication

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei204 – 2041Proton donorBy similarity
Active sitei312 – 3121NucleophileBy similarity

GO - Molecular functioni

  1. mannan endo-1,4-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

Protein family/group databases

mycoCLAPiMAN5A_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase B (EC:3.2.1.78)
Alternative name(s):
Endo-beta-1,4-mannanase B
Gene namesi
Name:manB
ORF Names:AN3297
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VI

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 387363Mannan endo-1,4-beta-mannosidase BPRO_0000393708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5B833.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
InParanoidiQ5B833.
OrthoDBiEOG7M3J90.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5B833-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLIHAVLGL LAGAAPALVA ASPAAPIGNG RDQVSKAVGR HFEIDGKVQY
60 70 80 90 100
FAGTNCWWLG NLLNDFEVEL AVSQIAETGY KVVRTWGFFG VNDPSNPGQP
110 120 130 140 150
VYYQVLNESL YEGGLGINYG SNGIRRLDTV VSLAERYDIQ LVLTFMNNWN
160 170 180 190 200
DFGGINIYSN AFGSNATTWY TDKKSQRAYR EYIKFIVNRY KGSSAIFAWE
210 220 230 240 250
LGNEPRCKGC DPSVIYNWAK SVSAYIKKLD KKHMVALGDE GWLCPPEGDG
260 270 280 290 300
TYAYDCSEGV DFVKNLEIET LDYGTFHLYP ESWGYNYSWG SEWVLQHDAI
310 320 330 340 350
GKRFNKPVVF EEYGTPLNHT QLERPWQLTT VKETQVAADF IWQFGTVLPV
360 370 380
EGTEWGDVNS IYYGTEEYEV LAVQHAWEMA RKKVPRH
Length:387
Mass (Da):43,725
Last modified:April 20, 2010 - v2
Checksum:i8CC8A4C1253E7823
GO

Sequence cautioni

The sequence CBF83007.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA63265.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490485 mRNA. Translation: ABF50861.1.
AACD01000055 Genomic DNA. Translation: EAA63265.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF83007.1. Sequence problems.
RefSeqiXP_660901.1. XM_655809.1.

Genome annotation databases

EnsemblFungiiCADANIAT00009761; CADANIAP00009761; CADANIAG00009761.
GeneIDi2873762.
KEGGiani:AN3297.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490485 mRNA. Translation: ABF50861.1.
AACD01000055 Genomic DNA. Translation: EAA63265.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF83007.1. Sequence problems.
RefSeqiXP_660901.1. XM_655809.1.

3D structure databases

ProteinModelPortaliQ5B833.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiMAN5A_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00009761; CADANIAP00009761; CADANIAG00009761.
GeneIDi2873762.
KEGGiani:AN3297.2.

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
InParanoidiQ5B833.
OrthoDBiEOG7M3J90.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. 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.

Entry informationi

Entry nameiMANB_EMENI
AccessioniPrimary (citable) accession number: Q5B833
Secondary accession number(s): C8VI04, Q1HFT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: January 7, 2015
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.