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P22533 (MANB_CALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-mannanase/endoglucanase A

Including the following 2 domains:

  1. Mannan endo-1,4-beta-mannosidase A
    EC=3.2.1.78
    Alternative name(s):
    Beta-mannanase
    Endo-1,4-mannanase
  2. Endo-1,4-beta-glucanase
    EC=3.2.1.4
    Alternative name(s):
    Cellulase
Gene names
Name:manA
OrganismCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifier44001 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length1331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degradation of hemicelluloses, the second most abundant polysaccharides in nature. Contains two catalytic domains with mannanase and endoglucanase activities.

Catalytic activity

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

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sequence similarities

In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.

In the C-terminal section; belongs to the glycosyl hydrolase 44 (cellulase J) family.

Contains 2 CBM3 (carbohydrate binding type-3) domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.

Temperature dependence:

Optimum temperature is 80 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 13311290Beta-mannanase/endoglucanase A
PRO_0000007899

Regions

Domain363 – 516154CBM3 1
Domain566 – 719154CBM3 2
Region42 – 325284Catalytic (mannanase)
Region781 – 1331551Catalytic (endoglucanase)
Compositional bias326 – 36136Pro/Ser/Thr-rich (PT box)
Compositional bias519 – 56446Pro/Ser/Thr-rich (PT box)
Compositional bias721 – 78060Pro/Ser/Thr-rich (PT box)

Sites

Active site1621Proton donor By similarity
Active site2571Nucleophile By similarity

Experimental info

Sequence conflict3381T → P Ref.2
Sequence conflict340 – 3467TPTPTPT → RQHQHRQ Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22533 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: FFBCA51BB8D8F0E0

FASTA1,331146,893
        10         20         30         40         50         60 
MRLKTKIRKK WLSVLCTVVF LLNILFIANV TILPKVGAAT SNDGVVKIDT STLIGTNHAH 

        70         80         90        100        110        120 
CWYRDRLDTA LRGIRSWGMN SVRVVLSNGY RWTKIPASEV ANIISLSRSL GFKAIILEVH 

       130        140        150        160        170        180 
DTTGYGEDGA ACSLAQAVEY WKEIKSVLDG NEDFVIINIG NEPYGNNNYQ NWVNDTKNAI 

       190        200        210        220        230        240 
KALRDAGFKH TIMVDAPNWG QDWSNTMRDN AQSIMEADPL RNLVFSIHMY GVYNTASKVE 

       250        260        270        280        290        300 
EYIKSFVDKG LPLVIGEFGH QHTDGDPDEE AIVRYAKQYK IGLFSWSWCG NSSYVGYLDM 

       310        320        330        340        350        360 
VNNWDPNNPT PWGQWYKTNA IGTSSTPTPT STVTPTPTPT PTPTPTVTAT PTPTPTPVST 

       370        380        390        400        410        420 
PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV DGERAQSAIS 

       430        440        450        460        470        480 
DWAQIGASNV TFKFVKLSSS VSGADYYLEI GFKSGAGQLQ PGKDTGEIQM RFNKDDWSNY 

       490        500        510        520        530        540 
NQGNDWSWIQ SMTSYGENEK VTAYIDGVLV WGQEPSGATP APAPTATPTP TPTVTPTPTV 

       550        560        570        580        590        600 
TPTPTVTATP TPTPTPTPTP VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI 

       610        620        630        640        650        660 
DLSRVTIRYW YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG 

       670        680        690        700        710        720 
QLQPGKDTGE IQIRFNKSDW SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG VLVWGQEPSG 

       730        740        750        760        770        780 
TTPSPTSTPT VTVTPTPTPT PTPTPTPTVT PTPTVTPTPT VTATPTPTPT PIPTVTPLPT 

       790        800        810        820        830        840 
ISPSPSVVEI TINTNAGRTQ ISPYIYGANQ DIEGVVHSAR RLGGNRLTGY NWENNFSNAG 

       850        860        870        880        890        900 
NDWYHSSDDY LCWSMGISGE DAKVPAAVVS KFHEYSLKNN AYSAVTLQMA GYVSKDNYGT 

       910        920        930        940        950        960 
VSENETAPSN RWAEVKFKKD APLSLNPDLN DNFVYMDEFI NYLINKYGMA SSPTGIKGYI 

       970        980        990       1000       1010       1020 
LDNEPDLWAS THPRIHPNKV TCKELIEKSV ELAKVIKTLD PSAEVFGYAS YGFMGYYSLQ 

      1030       1040       1050       1060       1070       1080 
DAPDWNQVKG EHRWFISWYL EQMKKASDSF GKRLLDVLDL HWYPEARGGN IRVCFDGEND 

      1090       1100       1110       1120       1130       1140 
TSKEVVIARM QAPRTLWDPT YKTSVKGQIT AGENSWINQW FSDYLPIIPN VKADIEKYYP 

      1150       1160       1170       1180       1190       1200 
GTKLAISEFD YGGRNHISGG IALADVLGIF GKYGVNFAAR WGDSGSYAAA AYNIYLNYDG 

      1210       1220       1230       1240       1250       1260 
KGSKYGNTNV SANTSDVENM PVYASINGQD DSELHIILIN RNYDQKLQVK INITSTPKYT 

      1270       1280       1290       1300       1310       1320 
KAEIYGFDSN SPEYKKMGNI DNIESNVFTL EVPKFNGVSH SITLDFNVSI KIIQNEVIKF 

      1330 
IRNLVFMRAL V 

« Hide

References

[1]"The beta-mannanase from 'Caldocellum saccharolyticum' is part of a multidomain enzyme."
Gibbs M.D., Saul D.J., Luthi E., Bergquist P.L.
Appl. Environ. Microbiol. 58:3864-3867(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum'."
Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L.
Appl. Environ. Microbiol. 57:694-700(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01257 Unassigned DNA. Translation: AAA71887.1.
M36063 Genomic DNA. Translation: AAA72861.1.
PIRA48954.

3D structure databases

ProteinModelPortalP22533.
SMRP22533. Positions 786-1298.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.
GH44. Glycoside Hydrolase Family 44.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2730.

Family and domain databases

Gene3D2.60.40.710. 2 hits.
3.20.20.80. 3 hits.
InterProIPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR024745. Glyco_hydro_44.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00942. CBM_3. 2 hits.
PF00150. Cellulase. 1 hit.
PF12891. Glyco_hydro_44. 1 hit.
[Graphical view]
SMARTSM01067. CBM_3. 2 hits.
[Graphical view]
SUPFAMSSF49384. SSF49384. 2 hits.
SSF51445. SSF51445. 3 hits.
PROSITEPS51172. CBM3. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANB_CALSA
AccessionPrimary (citable) accession number: P22533
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: December 11, 2013
This is version 92 of the entry and version 2 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