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P49425 (MANA_RHOM4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannan endo-1,4-beta-mannosidase

EC=3.2.1.78
Alternative name(s):
Endo-(1,4)-beta-mannanase
Gene names
Name:manA
Ordered Locus Names:Rmar_0016
OrganismRhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus obamensis) [Complete proteome] [HAMAP]
Taxonomic identifier518766 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeRhodothermus

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as endo-acting enzyme with a requirement for at least five sugar moieties for effective catalytic activity. Hydrolyzes carob-galactomannan (locust bean gum) effectively and to a smaller extent guar gum, but not yeast mannan. Ref.1

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.4. Ref.1

Temperature dependence:

Optimum temperature is 85 degrees Celsius.

Sequence caution

The sequence CAA62442.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Mannan endo-1,4-beta-mannosidase
PRO_0000057685

Regions

Domain17 – 137121CBM6

Sequences

Sequence LengthMass (Da)Tools
P49425 [UniParc].

Last modified January 19, 2010. Version 3.
Checksum: E977F92CEE320807

FASTA55863,120
        10         20         30         40         50         60 
MTLLLVWLIF TGVAGEIRLE AEDGELLGVA VDSTLTGYSG RGYVTGFDAP EDSVRFSFEA 

        70         80         90        100        110        120 
PRGVYRVVFG VSFSSRFASY ALRVDDWHQT GSLIKRGGGF FEASIGEIWL DEGAHTMAFQ 

       130        140        150        160        170        180 
LMNGALDYVR LEPVSYGPPA RPPAQLSDSQ ATASAQALFA FLLSEYGRHI LAGQQQNPYR 

       190        200        210        220        230        240 
RDFDAINYVR NVTGKEPALV SFDLIDYSPT REAHGVVHYQ TPEDWIAWAG RDGIVSLMWH 

       250        260        270        280        290        300 
WNAPTDLIED PSQDCYWWYG FYTRCTTFDV AAALADTSSE RYRLLLRDID VIAAQLQKFQ 

       310        320        330        340        350        360 
QADIPVLWRP LHEAAGGWFW WGAKGPEPFK QLWRLLYERL VHHHGLHNLI WVYTHEPGAA 

       370        380        390        400        410        420 
EWYPGDAYVD IVGRDVYADD PDALMRSDWN ELQTLFGGRK LVALTETGTL PDVEVITDYG 

       430        440        450        460        470        480 
IWWSWFSIWT DPFLRDVDPD RLTRVYHSER VLTRDELPDW RSYVLHATTV QPAGDLALAV 

       490        500        510        520        530        540 
YPNPGAGRLH VEVGLPVAAP VVVEVFNLLG QRVFQYQAGM QPAGLWRRAF ELALAPGVYL 

       550 
VQVRAGNLVA RRRWVSVR 

« Hide

References

« Hide 'large scale' references
[1]"A highly thermostable endo-(1,4)-beta-mannanase from the marine bacterium Rhodothermus marinus."
Politz O., Krah M., Thomsen K.K., Borriss R.
Appl. Microbiol. Biotechnol. 53:715-721(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Complete genome sequence of Rhodothermus marinus type strain (R-10)."
Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A., Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G., Pati A. expand/collapse author list , Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.
Stand. Genomic Sci. 1:283-291(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43812 / DSM 4252 / R-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X90947 Genomic DNA. Translation: CAA62442.1. Different initiation.
CP001807 Genomic DNA. Translation: ACY46925.1.
PIRT10748.
RefSeqYP_003289313.1. NC_013501.1.

3D structure databases

ProteinModelPortalP49425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING518766.Rmar_0016.

Protein family/group databases

CAZyCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACY46925; ACY46925; Rmar_0016.
GeneID8566638.
KEGGrmr:Rmar_0016.
PATRIC32314039. VBIRhoMar93821_0016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4124.
HOGENOMHOG000235025.
OrthoDBEOG66HVDV.

Enzyme and pathway databases

BioCycRMAR518766:GJJ8-18-MONOMER.
BRENDA3.2.1.78. 5425.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProIPR005084. CMB_fam6.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR026444. Secre_tail.
[Graphical view]
PfamPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSPR00739. GLHYDRLASE26.
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR04183. Por_Secre_tail. 1 hit.
PROSITEPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANA_RHOM4
AccessionPrimary (citable) accession number: P49425
Secondary accession number(s): D0MK12
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 19, 2010
Last modified: May 14, 2014
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries