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P22533

- MANB_CALSA

UniProt

P22533 - MANB_CALSA

Protein

Beta-mannanase/endoglucanase A

Gene

manA

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    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.

    pH dependencei

    Optimum pH is 6.

    Temperature dependencei

    Optimum temperature is 80 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei162 – 1621Proton donorBy similarity
    Active sitei257 – 2571NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro
    3. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH44. Glycoside Hydrolase Family 44.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-mannanase/endoglucanase A
    Including the following 2 domains:
    Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.78)
    Alternative name(s):
    Beta-mannanase
    Endo-1,4-mannanase
    Endo-1,4-beta-glucanase (EC:3.2.1.4)
    Alternative name(s):
    Cellulase
    Gene namesi
    Name:manA
    OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
    Taxonomic identifieri44001 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Sequence AnalysisAdd
    BLAST
    Chaini42 – 13311290Beta-mannanase/endoglucanase APRO_0000007899Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP22533.
    SMRiP22533. Positions 786-1298.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini363 – 516154CBM3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini566 – 719154CBM3 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 325284Catalytic (mannanase)Add
    BLAST
    Regioni781 – 1331551Catalytic (endoglucanase)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi326 – 36136Pro/Ser/Thr-rich (PT box)Add
    BLAST
    Compositional biasi519 – 56446Pro/Ser/Thr-rich (PT box)Add
    BLAST
    Compositional biasi721 – 78060Pro/Ser/Thr-rich (PT box)Add
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated
    In the C-terminal section; belongs to the glycosyl hydrolase 44 (cellulase J) family.Curated
    Contains 2 CBM3 (carbohydrate binding type-3) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2730.

    Family and domain databases

    Gene3Di2.60.40.710. 2 hits.
    3.20.20.80. 3 hits.
    InterProiIPR008965. 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]
    PfamiPF00942. CBM_3. 2 hits.
    PF00150. Cellulase. 1 hit.
    PF12891. Glyco_hydro_44. 1 hit.
    [Graphical view]
    SMARTiSM01067. CBM_3. 2 hits.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 2 hits.
    SSF51445. SSF51445. 3 hits.
    PROSITEiPS51172. CBM3. 2 hits.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P22533-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLKTKIRKK WLSVLCTVVF LLNILFIANV TILPKVGAAT SNDGVVKIDT     50
    STLIGTNHAH CWYRDRLDTA LRGIRSWGMN SVRVVLSNGY RWTKIPASEV 100
    ANIISLSRSL GFKAIILEVH DTTGYGEDGA ACSLAQAVEY WKEIKSVLDG 150
    NEDFVIINIG NEPYGNNNYQ NWVNDTKNAI KALRDAGFKH TIMVDAPNWG 200
    QDWSNTMRDN AQSIMEADPL RNLVFSIHMY GVYNTASKVE EYIKSFVDKG 250
    LPLVIGEFGH QHTDGDPDEE AIVRYAKQYK IGLFSWSWCG NSSYVGYLDM 300
    VNNWDPNNPT PWGQWYKTNA IGTSSTPTPT STVTPTPTPT PTPTPTVTAT 350
    PTPTPTPVST PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS 400
    RVTIRYWYTV DGERAQSAIS DWAQIGASNV TFKFVKLSSS VSGADYYLEI 450
    GFKSGAGQLQ PGKDTGEIQM RFNKDDWSNY NQGNDWSWIQ SMTSYGENEK 500
    VTAYIDGVLV WGQEPSGATP APAPTATPTP TPTVTPTPTV TPTPTVTATP 550
    TPTPTPTPTP VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI 600
    DLSRVTIRYW YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY 650
    LEIGFKSGAG QLQPGKDTGE IQIRFNKSDW SNYNQGNDWS WIQSMTSYGE 700
    NEKVTAYIDG VLVWGQEPSG TTPSPTSTPT VTVTPTPTPT PTPTPTPTVT 750
    PTPTVTPTPT VTATPTPTPT PIPTVTPLPT ISPSPSVVEI TINTNAGRTQ 800
    ISPYIYGANQ DIEGVVHSAR RLGGNRLTGY NWENNFSNAG NDWYHSSDDY 850
    LCWSMGISGE DAKVPAAVVS KFHEYSLKNN AYSAVTLQMA GYVSKDNYGT 900
    VSENETAPSN RWAEVKFKKD APLSLNPDLN DNFVYMDEFI NYLINKYGMA 950
    SSPTGIKGYI LDNEPDLWAS THPRIHPNKV TCKELIEKSV ELAKVIKTLD 1000
    PSAEVFGYAS YGFMGYYSLQ DAPDWNQVKG EHRWFISWYL EQMKKASDSF 1050
    GKRLLDVLDL HWYPEARGGN IRVCFDGEND TSKEVVIARM QAPRTLWDPT 1100
    YKTSVKGQIT AGENSWINQW FSDYLPIIPN VKADIEKYYP GTKLAISEFD 1150
    YGGRNHISGG IALADVLGIF GKYGVNFAAR WGDSGSYAAA AYNIYLNYDG 1200
    KGSKYGNTNV SANTSDVENM PVYASINGQD DSELHIILIN RNYDQKLQVK 1250
    INITSTPKYT KAEIYGFDSN SPEYKKMGNI DNIESNVFTL EVPKFNGVSH 1300
    SITLDFNVSI KIIQNEVIKF IRNLVFMRAL V 1331
    Length:1,331
    Mass (Da):146,893
    Last modified:July 1, 1993 - v2
    Checksum:iFFBCA51BB8D8F0E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti338 – 3381T → P(PubMed:2039230)Curated
    Sequence conflicti340 – 3467TPTPTPT → RQHQHRQ(PubMed:2039230)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01257 Unassigned DNA. Translation: AAA71887.1.
    M36063 Genomic DNA. Translation: AAA72861.1.
    PIRiA48954.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01257 Unassigned DNA. Translation: AAA71887.1 .
    M36063 Genomic DNA. Translation: AAA72861.1 .
    PIRi A48954.

    3D structure databases

    ProteinModelPortali P22533.
    SMRi P22533. Positions 786-1298.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH44. Glycoside Hydrolase Family 44.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG2730.

    Family and domain databases

    Gene3Di 2.60.40.710. 2 hits.
    3.20.20.80. 3 hits.
    InterProi IPR008965. 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 ]
    Pfami PF00942. CBM_3. 2 hits.
    PF00150. Cellulase. 1 hit.
    PF12891. Glyco_hydro_44. 1 hit.
    [Graphical view ]
    SMARTi SM01067. CBM_3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 2 hits.
    SSF51445. SSF51445. 3 hits.
    PROSITEi PS51172. CBM3. 2 hits.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiMANB_CALSA
    AccessioniPrimary (citable) accession number: P22533
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 93 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

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3