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Q5B7X2

- MANA_EMENI

UniProt

Q5B7X2 - MANA_EMENI

Protein

Mannan endo-1,4-beta-mannosidase A

Gene

manA

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
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    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.

    pH dependencei

    Optimum pH is 5.5.1 Publication

    Temperature dependencei

    Optimum temperature is 52 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei211 – 2111Proton 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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Protein family/group databases

    mycoCLAPiMAN5B_EMENI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.78)
    Alternative name(s):
    Endo-beta-1,4-mannanase A
    Gene namesi
    Name:manA
    Synonyms:man1
    ORF Names:AN3358
    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 383365Mannan endo-1,4-beta-mannosidase APRO_0000393706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B7X2.
    SMRiQ5B7X2. Positions 43-378.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3934.
    HOGENOMiHOG000169951.
    OMAiLWITSHA.
    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.

    Q5B7X2-1 [UniParc]FASTAAdd to Basket

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    MKFSQALLSL ASLALAAALP HASTPVYTPS TTPSPTPTPS ASGSFATTSG    50
    IQFVIDGEAG YFPGSNAYWI GFLKNNSDVD LVFDHMASSG LRILRVWGFN 100
    DVNTAPTDGS VYFQLHQDGK STINTGKDGL QRLDYVVHSA EKHGIKLIIN 150
    FVNYWDDYGG MNAYMRAYGG GDKADWFENE GIQAAYQAYV EAVVKRYINS 200
    TAVFAWELAN EPRCTGCEPS VLHNWIEKTS AFIKGLDEKH LVCIGDGSDG 250
    SYPFQYTEGS DFAAALTIDT IDFGTFHLYP DSWGTNNDWG KLWITSHAAA 300
    CAAAGKPCLF EEYGVTSNHC AIEKQWQNAA LNATGIAADL YWQYGDTLSS 350
    GPSPDDGNTF YYGSEEFECL VTNHVETIER SAK 383
    Length:383
    Mass (Da):41,789
    Last modified:April 26, 2005 - v1
    Checksum:i686126F8B2CF12C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490487 mRNA. Translation: ABF50863.1.
    AACD01000055 Genomic DNA. Translation: EAA63326.1.
    BN001306 Genomic DNA. Translation: CBF82875.1.
    RefSeqiXP_660962.1. XM_655870.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00009689; CADANIAP00009689; CADANIAG00009689.
    GeneIDi2874351.
    KEGGiani:AN3358.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490487 mRNA. Translation: ABF50863.1 .
    AACD01000055 Genomic DNA. Translation: EAA63326.1 .
    BN001306 Genomic DNA. Translation: CBF82875.1 .
    RefSeqi XP_660962.1. XM_655870.1.

    3D structure databases

    ProteinModelPortali Q5B7X2.
    SMRi Q5B7X2. Positions 43-378.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    mycoCLAPi MAN5B_EMENI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00009689 ; CADANIAP00009689 ; CADANIAG00009689 .
    GeneIDi 2874351.
    KEGGi ani:AN3358.2.

    Phylogenomic databases

    eggNOGi COG3934.
    HOGENOMi HOG000169951.
    OMAi LWITSHA.
    OrthoDBi EOG7M3J90.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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, BIOPHYSICOCHEMICAL PROPERTIES.
      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 nameiMANA_EMENI
    AccessioniPrimary (citable) accession number: Q5B7X2
    Secondary accession number(s): C8VHS1, Q1HFT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 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