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Q00012

- MANA_ASPAC

UniProt

Q00012 - MANA_ASPAC

Protein

Mannan endo-1,4-beta-mannosidase A

Gene

manA

Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.1 Publication

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5.0.1 Publication

    Temperature dependencei

    Optimum temperature is between 60 and 70 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei198 – 1981Proton donorBy similarity
    Active sitei306 – 3061NucleophileBy similarity

    GO - Molecular functioni

    1. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiMAN5A_ASPAC.

    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
    OrganismiAspergillus aculeatus
    Taxonomic identifieri5053 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    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 – 377359Mannan endo-1,4-beta-mannosidase APRO_5000142576Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ00012.
    SMRiQ00012. Positions 30-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    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.

    Q00012-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLSHMLLSL ASLGVATALP RTPNHNAATT AFPSTSGLHF TIDGKTGYFA    50
    GTNSYWIGFL TNNDDVDLVM SQLAASDLKI LRVWGFNDVN TKPTDGTVWY 100
    QLHANGTSTI NTGADGLQRL DYVVTSAEKY GVKLIINFVN EWTDYGGMQA 150
    YVTAYGAAAQ TDFYTNTAIQ AAYKNYIKAV VSRYSSSAAI FAWELANEPR 200
    CQGCDTSVLY NWISDTSKYI KSLDSKHLVT IGDEGFGLDV DSDGSYPYTY 250
    GEGLNFTKNL GISTIDFGTL HLYPDSWGTS YDWGNGWITA HAAACKAVGK 300
    PCLLEEYGVT SNHCAVESPW QQTAGNATGI SGDLYWQYGT TFSWGQSPND 350
    GNTFYYNTSD FTCLVTDHVA AINAQSK 377
    Length:377
    Mass (Da):41,082
    Last modified:November 1, 1996 - v1
    Checksum:i10E6477555BE3CA2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35487 mRNA. Translation: AAA67426.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35487 mRNA. Translation: AAA67426.1 .

    3D structure databases

    ProteinModelPortali Q00012.
    SMRi Q00012. Positions 30-373.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi MAN5A_ASPAC.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Expression cloning, purification and characterization of a beta-1,4-mannanase from Aspergillus aculeatus."
      Christgau S., Kauppinen S., Vind J., Kofod L.V., Dalboge H.
      Biochem. Mol. Biol. Int. 33:917-925(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: KSM 510.

    Entry informationi

    Entry nameiMANA_ASPAC
    AccessioniPrimary (citable) accession number: Q00012
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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