Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mannan endo-1,4-beta-mannosidase

Gene

manA

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan. Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides.2 Publications

Catalytic activityi

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

pH dependencei

Optimum pH is about 7.0.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciCJAP498211:GHIT-2761-MONOMER.

Protein family/group databases

CAZyiGH26. Glycoside Hydrolase Family 26.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase (EC:3.2.1.78)
Alternative name(s):
Mannanase A
Gene namesi
Name:manA
Synonyms:man26A
Ordered Locus Names:CJA_2770
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
ProteomesiUP000001036 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 387Sequence AnalysisPRO_0000012172
Chaini39 – 423385Mannan endo-1,4-beta-mannosidasePRO_0000012173Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_2770.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 473Combined sources
Helixi56 – 6813Combined sources
Turni69 – 713Combined sources
Beta strandi73 – 786Combined sources
Turni79 – 824Combined sources
Beta strandi91 – 933Combined sources
Helixi96 – 1016Combined sources
Beta strandi106 – 1116Combined sources
Helixi112 – 1143Combined sources
Helixi125 – 1339Combined sources
Beta strandi137 – 1415Combined sources
Turni147 – 1493Combined sources
Helixi150 – 1523Combined sources
Turni156 – 1594Combined sources
Turni169 – 1713Combined sources
Helixi178 – 19316Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi215 – 2184Combined sources
Turni222 – 2243Combined sources
Helixi227 – 24216Combined sources
Beta strandi249 – 2546Combined sources
Helixi264 – 2685Combined sources
Turni274 – 2763Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi283 – 2864Combined sources
Beta strandi288 – 2903Combined sources
Helixi292 – 31221Combined sources
Beta strandi320 – 3234Combined sources
Helixi325 – 3295Combined sources
Helixi337 – 34711Combined sources
Helixi351 – 3533Combined sources
Beta strandi355 – 3595Combined sources
Helixi385 – 3895Combined sources
Helixi392 – 40110Combined sources
Helixi408 – 4103Combined sources
Beta strandi419 – 4213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 42-422.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49424.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 26 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000274384.
OMAiFLYAYSP.
OrthoDBiEOG6V4G9N.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF51445. SSF51445. 1 hit.

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
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. Positions 42-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498211.CJA_2770.

Protein family/group databases

CAZyiGH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000274384.
OMAiFLYAYSP.
OrthoDBiEOG6V4G9N.

Enzyme and pathway databases

BioCyciCJAP498211:GHIT-2761-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP49424.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa."
    Braithwaite K.L., Black G.W., Hazlewood G.P., Ali B.R.S., Gilbert H.J.
    Biochem. J. 305:1005-1010(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-48, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PH DEPENDENCE.
  2. Gilbert H.J.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 364-423.
  3. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
    DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
    J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ueda107.
  4. "alpha-Galactosidase A from Pseudomonas fluorescens subsp. cellulosa: cloning, high level expression and its role in galactomannan hydrolysis."
    Halstead J.R., Fransen M.P., Eberhart R.Y., Park A.J., Gilbert H.J., Hazlewood G.P.
    FEMS Microbiol. Lett. 192:197-203(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

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: July 22, 2015
This is version 87 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

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.