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Reviewed, UniProtKB/Swiss-Prot P49425 (MANA_RHOMR)

Last modified June 16, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismRhodothermus marinus (Rhodothermus obamensis)
Taxonomic identifier29549 [NCBI]
Taxonomic lineageBacteriaBacteroidetesSphingobacteriaSphingobacterialesRhodothermaceaeRhodothermus

Protein attributes

Sequence length1021 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Temperature dependence:

Optimum temperature is 85 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10211021Mannan endo-1,4-beta-mannosidase
PRO_0000057685

Regions

Domain480 – 600121CBM6

Sequences

Sequence LengthMass (Da)Tools
P49425-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: A8F7B63109E0F715

FASTA1,021115,791
        10         20         30         40         50         60 
MAGPHRSRAA GPPPFAVDEH VALEMVAFRG EVFAGHGLLA DQRLIAHTGR PALNAQRITQ 

        70         80         90        100        110        120 
QKQRDQCRGQ RHRHHQGGRN LRKAHRTFHE HQSTQDQAHD APHGQQAKTG HEGLGHEHAQ 

       130        140        150        160        170        180 
AQHQQGQSNV VDRQDGEPVE AQHQKDGAQR AGNAPAGRVE LEQQPVEAQH QQQEGDVRIG 

       190        200        210        220        230        240 
KRRQNAFAPP ALDHVHGGPG RLQRHGLAVE RHVPAVQQHQ QRVQRGRQQI DHVLGHGLPG 

       250        260        270        280        290        300 
RQRLAFRDGP RRPVGVASPV LGQRPCPGHR IVQNLFRHGI DPCRVGRCRR SPSELHGMGC 

       310        320        330        340        350        360 
ADVRARGHGR HMRGQRDEHP GRGRPCARRR HVDDDRDRTP QEKLYDVARG LDEPARRVHF 

       370        380        390        400        410        420 
DDEADRSVFR GLAQPAPDEP EGRRRDRLVL QRQSVNHRRG RLSRHRQQHQ PQQQRPHGNQ 

       430        440        450        460        470        480 
AFLGKYEKRR RKPTACLKSL RRFPDKDAPV LYFVNQLEKT KRRMTLLLVW LIFTGVAGEI 

       490        500        510        520        530        540 
RLEAEDGELL GVAVDSTLTG YSGRGYVTGF DAPEDSVRFS FEAPRGVYRV VFGVSFSSRF 

       550        560        570        580        590        600 
ASYALRVDDW HQTGSLIKRG GGFFEASIGE IWLDEGAHTM AFQLMNGALD YVRLEPVSYG 

       610        620        630        640        650        660 
PPARPPAQLS DSQATASAQA LFAFLLSEYG RHILAGQQQN PYRRDFDAIN YVRNVTGKEP 

       670        680        690        700        710        720 
ALVSFDLIDY SPTREAHGVV HYQTPEDWIA WAGRDGIVSL MWHWNAPTDL IEDPSQDCYW 

       730        740        750        760        770        780 
WYGFYTRCTT FDVAAALADT SSERYRLLLR DIDVIAAQLQ KFQQADIPVL WRPLHEAAGG 

       790        800        810        820        830        840 
WFWWGAKGPE PFKQLWRLLY ERLVHHHGLH NLIWVYTHEP GAAEWYPGDA YVDIVGRDVY 

       850        860        870        880        890        900 
ADDPDALMRS DWNELQTLFG GRKLVALTET GTLPDVEVIT DYGIWWSWFS IWTDPFLRDV 

       910        920        930        940        950        960 
DPDRLTRVYH SERVLTRDEL PDWRSYVLHA TTVQPAGDLA LAVYPNPGAG RLHVEVGLPV 

       970        980        990       1000       1010       1020 
AAPVVVEVFN LLGQRVFQYQ AGMQPAGLWR RAFELALAPG VYLVQVRAGN LVARRRWVSV 


R 

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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: 10919332] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 43812 / R-10 / DSM 4252.

Cross-references

Sequence databases

X90947 Genomic DNA. Translation: CAA62442.1.
PIRT10748.

3D structure databases

ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA3.2.1.78. 1132.

Family and domain databases

InterProIPR005084. CBM_6.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSPR00739. GLHYDRLASE26.
PROSITEPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANA_RHOMR
AccessionPrimary (citable) accession number: P49425
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 15, 1998
Last modified: June 16, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents