Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P16218

- GUNH_CLOTH

UniProt

P16218 - GUNH_CLOTH

Protein

Endoglucanase H

Gene

celH

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei460 – 4601Proton donorBy similarity
    Active sitei565 – 5651NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: MENGO
    2. mannan endo-1,4-beta-mannosidase activity Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW
    2. substituted mannan metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciCTHE203119:GIW8-1525-MONOMER.
    MetaCyc:MONOMER-16422.

    Protein family/group databases

    CAZyiCBM11. Carbohydrate-Binding Module Family 11.
    GH26. Glycoside Hydrolase Family 26.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase H (EC:3.2.1.4)
    Alternative name(s):
    Cellulase H
    Endo-1,4-beta-glucanase H
    Short name:
    EgH
    Gene namesi
    Name:celH
    Ordered Locus Names:Cthe_1472
    OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
    Taxonomic identifieri203119 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
    ProteomesiUP000002145: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4444Add
    BLAST
    Chaini45 – 900856Endoglucanase HPRO_0000007854Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi203119.Cthe_1472.

    Structurei

    Secondary structure

    1
    900
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 365
    Helixi43 – 5311
    Beta strandi58 – 658
    Helixi70 – 8213
    Beta strandi86 – 927
    Helixi98 – 1025
    Turni103 – 1064
    Helixi107 – 12014
    Beta strandi124 – 1296
    Beta strandi134 – 1374
    Helixi150 – 16617
    Beta strandi172 – 1754
    Beta strandi178 – 1814
    Helixi196 – 1983
    Beta strandi200 – 2089
    Turni214 – 2163
    Helixi222 – 23312
    Beta strandi236 – 2383
    Beta strandi240 – 2478
    Helixi254 – 26815
    Beta strandi272 – 2787
    Beta strandi281 – 2855
    Helixi292 – 30110
    Beta strandi656 – 6627
    Beta strandi664 – 6674
    Beta strandi671 – 6755
    Beta strandi679 – 6868
    Beta strandi688 – 69811
    Beta strandi704 – 7107
    Beta strandi721 – 7288
    Beta strandi730 – 7323
    Beta strandi736 – 7438
    Beta strandi747 – 75812
    Beta strandi765 – 7706
    Helixi771 – 7733
    Beta strandi788 – 7903
    Beta strandi795 – 80612
    Beta strandi809 – 81911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V0AX-ray1.98A655-821[»]
    2BV9X-ray1.50A26-304[»]
    2BVDX-ray1.60A26-304[»]
    2CIPX-ray1.40A26-304[»]
    2CITX-ray1.40A26-304[»]
    2LRONMR-A655-821[»]
    2LRPNMR-A655-821[»]
    2V3GX-ray1.20A26-305[»]
    2VI0X-ray1.51A26-304[»]
    ProteinModelPortaliP16218.
    SMRiP16218. Positions 29-304, 655-821.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16218.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini655 – 900246CBM11Add
    BLAST
    Repeati833 – 856241Add
    BLAST
    Repeati872 – 895242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 630586CatalyticBy similarityAdd
    BLAST
    Regioni833 – 895632 X 24 AA approximate repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi631 – 65424Pro/Thr-rich (linker)Add
    BLAST

    Domaini

    A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

    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 26 family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    KOiK01179.
    OMAiGSANEIR.
    OrthoDBiEOG66F040.

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR005087. CBM_fam11.
    IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR022790. EndoGluc_H/Glyco_hydro_26.
    IPR008979. Galactose-bd-like.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF03425. CBM_11. 1 hit.
    PF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF02156. Glyco_hydro_26. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 2 hits.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16218-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKRLLVSFL VLSIIVGLLS FQSLGNYNSG LKIGAWVGTQ PSESAIKSFQ    50
    ELQGRKLDIV HQFINWSTDF SWVRPYADAV YNNGSILMIT WEPWEYNTVD 100
    IKNGKADAYI TRMAQDMKAY GKEIWLRPLH EANGDWYPWA IGYSSRVNTN 150
    ETYIAAFRHI VDIFRANGAT NVKWVFNVNC DNVGNGTSYL GHYPGDNYVD 200
    YTSIDGYNWG TTQSWGSQWQ SFDQVFSRAY QALASINKPI IIAEFASAEI 250
    GGNKARWITE AYNSIRTSYN KVIAAVWFHE NKETDWRINS SPEALAAYRE 300
    AIGAGSSNPT PTPTWTSTPP SSSPKAVDPF EMVRKMGMGT NLGNTLEAPY 350
    EGSWSKSAME YYFDDFKAAG YKNVRIPVRW DNHTMRTYPY TIDKAFLDRV 400
    EQVVDWSLSR GFVTIINSHH DDWIKEDYNG NIERFEKIWE QIAERFKNKS 450
    ENLLFEIMNE PFGNITDEQI DDMNSRILKI IRKTNPTRIV IIGGGYWNSY 500
    NTLVNIKIPD DPYLIGTFHY YDPYEFTHKW RGTWGTQEDM DTVVRVFDFV 550
    KSWSDRNNIP VYFGEFAVMA YADRTSRVKW YDFISDAALE RGFACSVWDN 600
    GVFGSLDNDM AIYNRDTRTF DTEILNALFN PGTYPSYSPK PSPTPRPTKP 650
    PVTPAVGEKM LDDFEGVLNW GSYSGEGAKV STKIVSGKTG NGMEVSYTGT 700
    TDGYWGTVYS LPDGDWSKWL KISFDIKSVD GSANEIRFMI AEKSINGVGD 750
    GEHWVYSITP DSSWKTIEIP FSSFRRRLDY QPPGQDMSGT LDLDNIDSIH 800
    FMYANNKSGK FVVDNIKLIG ATSDPTPSIK HGDLNFDNAV NSTDLLMLKR 850
    YILKSLELGT SEQEEKFKKA ADLNRDNKVD STDLTILKRY LLKAISEIPI 900
    Length:900
    Mass (Da):102,416
    Last modified:April 1, 1990 - v1
    Checksum:i973AFB1954FC246B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31903 Genomic DNA. Translation: AAA23225.1.
    CP000568 Genomic DNA. Translation: ABN52701.1.
    PIRiJH0157.
    RefSeqiWP_011838089.1. NC_009012.1.
    YP_001037894.1. NC_009012.1.

    Genome annotation databases

    EnsemblBacteriaiABN52701; ABN52701; Cthe_1472.
    GeneIDi4810622.
    KEGGicth:Cthe_1472.
    PATRICi19516761. VBICloThe47081_1560.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31903 Genomic DNA. Translation: AAA23225.1 .
    CP000568 Genomic DNA. Translation: ABN52701.1 .
    PIRi JH0157.
    RefSeqi WP_011838089.1. NC_009012.1.
    YP_001037894.1. NC_009012.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V0A X-ray 1.98 A 655-821 [» ]
    2BV9 X-ray 1.50 A 26-304 [» ]
    2BVD X-ray 1.60 A 26-304 [» ]
    2CIP X-ray 1.40 A 26-304 [» ]
    2CIT X-ray 1.40 A 26-304 [» ]
    2LRO NMR - A 655-821 [» ]
    2LRP NMR - A 655-821 [» ]
    2V3G X-ray 1.20 A 26-305 [» ]
    2VI0 X-ray 1.51 A 26-304 [» ]
    ProteinModelPortali P16218.
    SMRi P16218. Positions 29-304, 655-821.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 203119.Cthe_1472.

    Protein family/group databases

    CAZyi CBM11. Carbohydrate-Binding Module Family 11.
    GH26. Glycoside Hydrolase Family 26.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN52701 ; ABN52701 ; Cthe_1472 .
    GeneIDi 4810622.
    KEGGi cth:Cthe_1472.
    PATRICi 19516761. VBICloThe47081_1560.

    Phylogenomic databases

    eggNOGi COG2730.
    KOi K01179.
    OMAi GSANEIR.
    OrthoDBi EOG66F040.

    Enzyme and pathway databases

    BioCyci CTHE203119:GIW8-1525-MONOMER.
    MetaCyc:MONOMER-16422.

    Miscellaneous databases

    EvolutionaryTracei P16218.

    Family and domain databases

    Gene3Di 1.10.1330.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR005087. CBM_fam11.
    IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR022790. EndoGluc_H/Glyco_hydro_26.
    IPR008979. Galactose-bd-like.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF03425. CBM_11. 1 hit.
    PF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF02156. Glyco_hydro_26. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 2 hits.
    SSF63446. SSF63446. 1 hit.
    PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and deletion analysis of the cellulase-encoding gene celH of Clostridium thermocellum."
      Yaguee E., Beguin P., Aubert J.-P.
      Gene 89:61-67(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.

    Entry informationi

    Entry nameiGUNH_CLOTH
    AccessioniPrimary (citable) accession number: P16218
    Secondary accession number(s): A3DFH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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