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Protein

Mannan endo-1,4-beta-mannosidase A

Gene

man1

Organism
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and ivory nut mannan, releasing mainly tri- and disaccharides (PubMed:7793911, Ref. 3, Ref. 4, PubMed:8529653). Also has transglycosylation activity. Transglycosylation of two mannotrioses into a mannohexaose is the major transglycosylation route (PubMed:8529653, Ref. 7, PubMed:24950755).6 Publications

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.3 Publications

Kineticsi

  1. KM=0.0015 mg/ml for locust bean gum mannan1 Publication
  2. KM=0.6 mg/ml for locust bean gum mannan1 Publication
  3. KM=0.25 mM for 4-methylumbelliferyl-mannotrioside1 Publication
  4. KM=0.31 mM for mannotetraose1 Publication
  5. KM=0.08 mM for mannopentaose1 Publication
  6. KM=0.05 mM for mannohexaose1 Publication

    pH dependencei

    Optimum pH is 5.0. Stable from pH 2.5 to 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 75 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei196Proton donor/acceptor1 Publication1
    Sitei198Important for transglycosylation activity1 Publication1
    Binding sitei232SubstrateCombined sources1 Publication1
    Binding sitei274SubstrateCombined sources1 Publication1
    Active sitei303Nucleophile1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosidase, Hydrolase

    Protein family/group databases

    CAZyiCBM1. Carbohydrate-Binding Module Family 1.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.783 Publications)
    Alternative name(s):
    Beta-mannanase 5A
    Short name:
    Man5A1 Publication
    Beta-mannanase I/II1 Publication
    Short name:
    BMANI
    Short name:
    BMANII
    Endo-beta-1,4-mannanase A
    Gene namesi
    Name:man11 Publication
    OrganismiHypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
    Taxonomic identifieri1344414 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma
    Proteomesi
    • UP000024376 Componenti: Unassembled WGS sequence

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi198R → K: Shows an altered product profile, producing mannotriose and mannose from mannotetraose, compared to predominantly mannobiose in the wild type. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 19Sequence analysisAdd BLAST19
    PropeptideiPRO_000044127820 – 271 Publication8
    ChainiPRO_500432268328 – 437Mannan endo-1,4-beta-mannosidase AAdd BLAST410

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi53 ↔ 56Combined sources1 Publication
    GlycosylationiCAR_5009973567157N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    GlycosylationiCAR_5009973566184N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Disulfide bondi199 ↔ 202Combined sources1 Publication
    GlycosylationiCAR_5009973568277N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Disulfide bondi292 ↔ 299Combined sources1 Publication
    Disulfide bondi311 ↔ 361Combined sources1 Publication
    GlycosylationiCAR_5009973565355N-linked (GlcNAc...) asparagineCombined sources1 Publication1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi51453.JGI56996.

    Structurei

    Secondary structure

    1437
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi33 – 35Combined sources3
    Beta strandi38 – 41Combined sources4
    Beta strandi44 – 46Combined sources3
    Beta strandi48 – 52Combined sources5
    Helixi54 – 58Combined sources5
    Helixi62 – 74Combined sources13
    Beta strandi79 – 81Combined sources3
    Beta strandi87 – 90Combined sources4
    Beta strandi99 – 101Combined sources3
    Turni113 – 116Combined sources4
    Helixi117 – 129Combined sources13
    Beta strandi132 – 137Combined sources6
    Beta strandi139 – 142Combined sources4
    Helixi146 – 154Combined sources9
    Helixi160 – 163Combined sources4
    Helixi165 – 182Combined sources18
    Beta strandi188 – 193Combined sources6
    Helixi205 – 221Combined sources17
    Beta strandi223 – 228Combined sources6
    Helixi243 – 245Combined sources3
    Beta strandi246 – 250Combined sources5
    Helixi253 – 257Combined sources5
    Beta strandi264 – 269Combined sources6
    Helixi271 – 274Combined sources4
    Helixi281 – 294Combined sources14
    Beta strandi299 – 304Combined sources6
    Helixi310 – 322Combined sources13
    Beta strandi327 – 333Combined sources7
    Helixi357 – 362Combined sources6
    Helixi364 – 370Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1QNOX-ray2.00A28-371[»]
    1QNPX-ray1.50A28-371[»]
    1QNQX-ray1.65A28-371[»]
    1QNRX-ray1.40A28-371[»]
    1QNSX-ray1.50A28-371[»]
    ProteinModelPortaliQ99036.
    SMRiQ99036.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99036.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini400 – 435CBM1PROSITE-ProRule annotationAdd BLAST36

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni28 – 376Catalytic1 PublicationAdd BLAST349
    Regioni196 – 198Substrate bindingCombined sources1 Publication3
    Regioni377 – 399Linker1 PublicationAdd BLAST23

    Domaini

    The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence (Probable). The CBM binds to cellulose but not to mannan, and increases the mannan-hydrolysis of complex substrates (PubMed:12523968).1 Publication1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG410IIG3. Eukaryota.
    COG3934. LUCA.

    Family and domain databases

    InterProiView protein in InterPro
    IPR035971. CBD_sf.
    IPR000254. Cellulose-bd_dom_fun.
    IPR001547. Glyco_hydro_5.
    IPR017853. Glycoside_hydrolase_SF.
    PfamiView protein in Pfam
    PF00734. CBM_1. 1 hit.
    PF00150. Cellulase. 1 hit.
    ProDomiView protein in ProDom or Entries sharing at least one domain
    PD001821. CBD_fun. 1 hit.
    SMARTiView protein in SMART
    SM00236. fCBD. 1 hit.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEiView protein in PROSITE
    PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q99036-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMMLSKSLLS AATAASALAA VLQPVPRASS FVTISGTQFN IDGKVGYFAG
    60 70 80 90 100
    TNCYWCSFLT NHADVDSTFS HISSSGLKVV RVWGFNDVNT QPSPGQIWFQ
    110 120 130 140 150
    KLSATGSTIN TGADGLQTLD YVVQSAEQHN LKLIIPFVNN WSDYGGINAY
    160 170 180 190 200
    VNAFGGNATT WYTNTAAQTQ YRKYVQAVVS RYANSTAIFA WELGNEPRCN
    210 220 230 240 250
    GCSTDVIVQW ATSVSQYVKS LDSNHLVTLG DEGLGLSTGD GAYPYTYGEG
    260 270 280 290 300
    TDFAKNVQIK SLDFGTFHLY PDSWGTNYTW GNGWIQTHAA ACLAAGKPCV
    310 320 330 340 350
    FEEYGAQQNP CTNEAPWQTT SLTTRGMGGD MFWQWGDTFA NGAQSNSDPY
    360 370 380 390 400
    TVWYNSSNWQ CLVKNHVDAI NGGTTTPPPV SSTTTTSSRT SSTPPPPGGS
    410 420 430
    CSPLYGQCGG SGYTGPTCCA QGTCIYSNYW YSQCLNT
    Length:437
    Mass (Da):47,053
    Last modified:November 1, 1996 - v1
    Checksum:i17513DADE12654A7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L25310 mRNA. Translation: AAA34208.1.
    KI911141 Genomic DNA. Translation: ETS04541.1.

    Genome annotation databases

    EnsemblFungiiETS04541; ETS04541; M419DRAFT_122377.

    Similar proteinsi

    Entry informationi

    Entry nameiMANA_HYPJR
    AccessioniPrimary (citable) accession number: Q99036
    Secondary accession number(s): A0A024SIJ3
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2017
    Last sequence update: November 1, 1996
    Last modified: October 25, 2017
    This is version 97 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families