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Protein

Mannan endo-1,4-beta-mannosidase

Gene

manA

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the endo hydrolysis of beta-1,4-linked mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall (PubMed:11382747). Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides (PubMed:7848261) (PubMed:8973192). It displays tight specificity for mannose at both the -2 and the -1 subsites (PubMed:19441796). Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan (PubMed:11064195).5 Publications

Catalytic activityi

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

Kineticsi

Kcat is 14.7 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMed:8973192). Kcat is 20 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMed:11382747). Kcat is 1759 sec(-1) for mannanase activity with carob galactomannan as substrate (PubMed:8973192). Kcat is 2904 sec(-1) for mannanase activity with carob galactomannan as substrate (PubMed:11382747). Kcat is 3861 sec(-1) for mannanase activity with mannotetraose as substrate (PubMed:8973192). Kcat is 280000 min(-1) for mannanase activity with galactomannan as substrate (PubMed:19441796). Kcat is 400000 min(-1) for mannanase activity with glucomannan as substrate (PubMed:19441796).3 Publications

Manual assertion based on experiment ini

  1. KM=0.9 mg/ml for carob galactomannan1 Publication
  2. KM=2.8 mg/ml for glucomannan1 Publication
  3. KM=3.2 mg/ml for galactomannan1 Publication
  4. KM=9.3 µM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)1 Publication
  5. KM=12.3 µM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)1 Publication

    pH dependencei

    Optimum pH is about 7.0.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei121Substrate2 Publications1
    Binding sitei143Substrate3 Publications1
    Binding sitei162Substrate1 Publication1 Publication1
    Sitei211Plays an important role in maintaining the position of the catalytic nucleophile1 Publication1 Publication1
    Active sitei212Proton donor4 Publications1
    Binding sitei217Substrate1 Publication1
    Binding sitei285Substrate2 Publications1
    Active sitei320Nucleophile2 Publications1
    Binding sitei377Substrate3 Publications1

    GO - Molecular functioni

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

    GO - Biological processi

    • galactomannan metabolic process Source: UniProtKB
    • glucomannan metabolic process Source: UniProtKB
    • polysaccharide catabolic process Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH26. Glycoside Hydrolase Family 26.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannan endo-1,4-beta-mannosidase1 Publication (EC:3.2.1.784 Publications)
    Alternative name(s):
    Mannanase 26A1 Publication
    Short name:
    Man26A1 Publication
    Mannanase A1 Publication
    Short name:
    ManA1 Publication
    Gene namesi
    Name:manA1 Publication
    Synonyms:man26A
    Ordered Locus Names:CJA_2770
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
    Proteomesi
    • UP000001036 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi121E → A: Strong decrease of mannanase activity against both oligosaccharides and polysaccharides. 1 Publication1
    Mutagenesisi143H → A: Very low mannanase activity against both mannans and mannooligosaccharides. 1 Publication1
    Mutagenesisi156W → A: Similar to the wild-type. 1 Publication1
    Mutagenesisi162W → A: The mannanase activity is 95, 70, and 30-fold less active than the wild-type against mannotriose, mannotetraose and mannohexaose, respectively. 1 Publication1
    Mutagenesisi211H → A: Causes a 100- and 700-fold decrease in mannanase activity against carob galactomannans and mannotetraose, respectively, but only a 6-fold reduction in mannanase activity against 2,4-DNPM. 1 Publication1
    Mutagenesisi212E → A: Causes a dramatic decrease in the catalytic efficiency against carob galactomannan, azo-carob galactomannan, mannotetraose and 2,4-DNPM. 2 Publications1
    Mutagenesisi212E → D: 10-fold decrease of the catalytic efficiency against 2,4-DNPM. 1 Publication1
    Mutagenesisi217W → A: Lack of mannanase activity against both mannotriose and mannotetraose. 1 Publication1
    Mutagenesisi278D → A: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
    Mutagenesisi278D → E: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
    Mutagenesisi283D → A: Retains significant activity against mannotetraose and azo-carob galactomannan. Lack of activity against all substrates; when associated with A-320. 2 Publications1
    Mutagenesisi283D → E: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
    Mutagenesisi285Y → A: Reduction of the catalytic efficiency with carob galactomannan and 2,4-DNPM. 1 Publication1
    Mutagenesisi320E → A: Does not alter the affinity against carob galactomannan, azo-carob galactomannan, mannotetraose and 2,4-DNPM. Lack of activity against all substrates; when associated with A-283. 2 Publications1
    Mutagenesisi320E → D: Causes a dramatic decrease in the catalytic efficiency against mannotetraose. 1 Publication1
    Mutagenesisi320E → G: Lack of activity against all substrates. 2 Publications1
    Mutagenesisi360W → A: Lack of activity against all substrates. 1 Publication1
    Mutagenesisi361R → A: Strong decrease of mannanase activity against oligosaccharides, while the reduction in the rate of polysaccharide hydrolysis is more modest. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units; when associated with A-377. 1 Publication1
    Mutagenesisi377H → A: 100-fold decrease in the activity of the mannanase against mannotetraose and 4-nitrophenyl-beta-D-Man2. It hydrolyzes polysaccharides only 10-20-fold less efficiently than the wild-type. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units; when associated with A-361. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 27PROSITE-ProRule annotation1 PublicationAdd BLAST27
    ChainiPRO_000001217328 – 423Mannan endo-1,4-beta-mannosidaseAdd BLAST396

    Proteomic databases

    PRIDEiP49424.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi498211.CJA_2770.

    Structurei

    Secondary structure

    1423
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi45 – 47Combined sources3
    Helixi56 – 68Combined sources13
    Turni69 – 71Combined sources3
    Beta strandi73 – 78Combined sources6
    Turni79 – 82Combined sources4
    Beta strandi91 – 93Combined sources3
    Helixi96 – 101Combined sources6
    Beta strandi106 – 111Combined sources6
    Helixi112 – 114Combined sources3
    Helixi125 – 133Combined sources9
    Beta strandi137 – 141Combined sources5
    Turni147 – 149Combined sources3
    Helixi150 – 152Combined sources3
    Turni156 – 159Combined sources4
    Turni169 – 171Combined sources3
    Helixi178 – 193Combined sources16
    Beta strandi205 – 208Combined sources4
    Beta strandi215 – 218Combined sources4
    Turni222 – 224Combined sources3
    Helixi227 – 242Combined sources16
    Beta strandi249 – 254Combined sources6
    Helixi264 – 268Combined sources5
    Turni274 – 276Combined sources3
    Beta strandi278 – 280Combined sources3
    Beta strandi283 – 286Combined sources4
    Beta strandi288 – 290Combined sources3
    Helixi292 – 312Combined sources21
    Beta strandi320 – 323Combined sources4
    Helixi325 – 329Combined sources5
    Helixi337 – 347Combined sources11
    Helixi351 – 353Combined sources3
    Beta strandi355 – 359Combined sources5
    Helixi385 – 389Combined sources5
    Helixi392 – 401Combined sources10
    Helixi408 – 410Combined sources3
    Beta strandi419 – 421Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1GVYX-ray1.70A39-363[»]
    1GW1X-ray1.65A43-421[»]
    1J9YX-ray1.85A39-423[»]
    1ODZX-ray1.40A/B39-423[»]
    1R7OX-ray1.85A29-423[»]
    2WHMX-ray1.50A39-423[»]
    ProteinModelPortaliP49424.
    SMRiP49424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49424.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini56 – 409GH26PROSITE-ProRule annotationAdd BLAST354

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni360 – 361Substrate binding3 Publications2

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 26 family.PROSITE-ProRule annotationCurated
    Contains 1 GH26 (glycosyl hydrolase family 26) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105D3P. Bacteria.
    COG4124. LUCA.
    HOGENOMiHOG000274384.
    KOiK01218.
    OMAiGHEMINE.
    OrthoDBiPOG091H0E82.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR022790. GH26_dom.
    IPR000805. Glyco_hydro_26.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR40079. PTHR40079. 1 hit.
    PfamiPF02156. Glyco_hydro_26. 1 hit.
    [Graphical view]
    PRINTSiPR00739. GLHYDRLASE26.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS51764. GH26. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49424-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTITTARLP WAAQSFALGI CLIALLGCNH AANKSSASRA DVKPVTVKLV
    60 70 80 90 100
    DSQATMETRS LFAFMQEQRR HSIMFGHQHE TTQGLTITRT DGTQSDTFNA
    110 120 130 140 150
    VGDFAAVYGW DTLSIVAPKA EGDIVAQVKK AYARGGIITV SSHFDNPKTD
    160 170 180 190 200
    TQKGVWPVGT SWDQTPAVVD SLPGGAYNPV LNGYLDQVAE WANNLKDEQG
    210 220 230 240 250
    RLIPVIFRLY HENTGSWFWW GDKQSTPEQY KQLFRYSVEY LRDVKGVRNF
    260 270 280 290 300
    LYAYSPNNFW DVTEANYLER YPGDEWVDVL GFDTYGPVAD NADWFRNVVA
    310 320 330 340 350
    NAALVARMAE ARGKIPVISE IGIRAPDIEA GLYDNQWYRK LISGLKADPD
    360 370 380 390 400
    AREIAFLLVW RNAPQGVPGP NGTQVPHYWV PANRPENINN GTLEDFQAFY
    410 420
    ADEFTAFNRD IEQVYQRPTL IVK
    Length:423
    Mass (Da):47,487
    Last modified:July 5, 2005 - v2
    Checksum:iEFDAB597F10BA3DD
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X82179 Genomic DNA. Translation: CAA57670.2.
    CP000934 Genomic DNA. Translation: ACE82849.1.
    PIRiS53374.
    RefSeqiWP_012488364.1. NC_010995.1.

    Genome annotation databases

    EnsemblBacteriaiACE82849; ACE82849; CJA_2770.
    KEGGicja:CJA_2770.
    PATRICi21328934. VBICelJap122165_2735.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X82179 Genomic DNA. Translation: CAA57670.2.
    CP000934 Genomic DNA. Translation: ACE82849.1.
    PIRiS53374.
    RefSeqiWP_012488364.1. NC_010995.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1GVYX-ray1.70A39-363[»]
    1GW1X-ray1.65A43-421[»]
    1J9YX-ray1.85A39-423[»]
    1ODZX-ray1.40A/B39-423[»]
    1R7OX-ray1.85A29-423[»]
    2WHMX-ray1.50A39-423[»]
    ProteinModelPortaliP49424.
    SMRiP49424.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi498211.CJA_2770.

    Protein family/group databases

    CAZyiGH26. Glycoside Hydrolase Family 26.

    Proteomic databases

    PRIDEiP49424.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACE82849; ACE82849; CJA_2770.
    KEGGicja:CJA_2770.
    PATRICi21328934. VBICelJap122165_2735.

    Phylogenomic databases

    eggNOGiENOG4105D3P. Bacteria.
    COG4124. LUCA.
    HOGENOMiHOG000274384.
    KOiK01218.
    OMAiGHEMINE.
    OrthoDBiPOG091H0E82.

    Miscellaneous databases

    EvolutionaryTraceiP49424.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR022790. GH26_dom.
    IPR000805. Glyco_hydro_26.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR40079. PTHR40079. 1 hit.
    PfamiPF02156. Glyco_hydro_26. 1 hit.
    [Graphical view]
    PRINTSiPR00739. GLHYDRLASE26.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS51764. GH26. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMANA_CELJU
    AccessioniPrimary (citable) accession number: P49424
    Secondary accession number(s): B3PBK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: July 5, 2005
    Last modified: November 2, 2016
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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

    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 one 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.