Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P37700

- GUNG_CLOCE

UniProt

P37700 - GUNG_CLOCE

(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)

Protein

Endoglucanase G

Gene

celCCG

Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei408 – 4081By similarity
Active sitei446 – 4461By similarity
Active sitei455 – 4551By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCCEL394503:GJET-752-MONOMER.
UniPathwayiUPA00696.

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase G (EC:3.2.1.4)
Alternative name(s):
Cellulase G
EGCCG
Endo-1,4-beta-glucanase G
Gene namesi
Name:celCCG
Ordered Locus Names:Ccel_0731
OrganismiClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Taxonomic identifieri394503 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001349: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 725690Endoglucanase GPRO_0000007947Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi394503.Ccel_0731.

Structurei

Secondary structure

1
725
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 5515
Beta strandi65 – 684
Turni74 – 774
Helixi78 – 803
Beta strandi91 – 933
Helixi98 – 12225
Helixi125 – 14117
Beta strandi149 – 1546
Helixi156 – 1605
Helixi166 – 1683
Beta strandi175 – 1784
Beta strandi180 – 1823
Helixi185 – 20218
Turni203 – 2053
Helixi207 – 22721
Turni235 – 2395
Helixi246 – 26015
Helixi263 – 2719
Helixi272 – 2754
Beta strandi282 – 2854
Helixi297 – 30812
Helixi311 – 32414
Beta strandi345 – 3473
Helixi348 – 36417
Helixi370 – 3723
Helixi373 – 38816
Turni389 – 3913
Beta strandi399 – 4024
Helixi410 – 4134
Beta strandi416 – 4183
Beta strandi422 – 4254
Helixi451 – 4544
Helixi458 – 47518
Beta strandi493 – 50412
Beta strandi507 – 51610
Beta strandi527 – 5359
Helixi537 – 5415
Helixi546 – 5483
Beta strandi549 – 5524
Beta strandi556 – 5583
Beta strandi567 – 5704
Helixi571 – 5733
Beta strandi575 – 5817
Beta strandi589 – 5913
Turni592 – 5954
Beta strandi596 – 6049
Helixi614 – 6163
Helixi618 – 6203
Beta strandi625 – 6284
Beta strandi633 – 6353
Beta strandi637 – 6393
Beta strandi642 – 6465

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G87X-ray1.60A/B36-649[»]
1GA2X-ray1.70A/B36-649[»]
1K72X-ray1.80A/B36-649[»]
1KFGX-ray1.90A/B36-649[»]
ProteinModelPortaliP37700.
SMRiP37700. Positions 37-649.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37700.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini489 – 650162CBM3PROSITE-ProRule annotationAdd
BLAST
Repeati664 – 687241Add
BLAST
Repeati696 – 719242Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni664 – 719562 X 24 AA approximate repeatsAdd
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

Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG05134.
HOGENOMiHOG000021032.
OMAiRKEVQFR.
OrthoDBiEOG6KQ6BP.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.40.710. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR016134. Cellulos_enz_dockerin_1.
IPR018242. Dockerin_1.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamiPF00942. CBM_3. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTiSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS51172. CBM3. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P37700-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKTKRKLTK AIGVALSISI LSSLVSFIPQ TNTYAAGTYN YGEALQKSIM
60 70 80 90 100
FYEFQRSGDL PADKRDNWRD DSGMKDGSDV GVDLTGGWYD AGDHVKFNLP
110 120 130 140 150
MSYTSAMLAW SLYEDKDAYD KSGQTKYIMD GIKWANDYFI KCNPTPGVYY
160 170 180 190 200
YQVGDGGKDH SWWGPAEVMQ MERPSFKVDA SKPGSAVCAS TAASLASAAV
210 220 230 240 250
VFKSSDPTYA EKCISHAKNL FDMADKAKSD AGYTAASGYY SSSSFYDDLS
260 270 280 290 300
WAAVWLYLAT NDSTYLDKAE SYVPNWGKEQ QTDIIAYKWG QCWDDVHYGA
310 320 330 340 350
ELLLAKLTNK QLYKDSIEMN LDFWTTGVNG TRVSYTPKGL AWLFQWGSLR
360 370 380 390 400
HATTQAFLAG VYAEWEGCTP SKVSVYKDFL KSQIDYALGS TGRSFVVGYG
410 420 430 440 450
VNPPQHPHHR TAHGSWTDQM TSPTYHRHTI YGALVGGPDN ADGYTDEINN
460 470 480 490 500
YVNNEIACDY NAGFTGALAK MYKHSGGDPI PNFKAIEKIT NDEVIIKAGL
510 520 530 540 550
NSTGPNYTEI KAVVYNQTGW PARVTDKISF KYFMDLSEIV AAGIDPLSLV
560 570 580 590 600
TSSNYSEGKN TKVSGVLPWD VSNNVYYVNV DLTGENIYPG GQSACRREVQ
610 620 630 640 650
FRIAAPQGTT YWNPKNDFSY DGLPTTSTVN TVTNIPVYDN GVKVFGNEPA
660 670 680 690 700
GGSENPDPEI LYGDVNSDKN VDALDFAALK KYLLGGTSSI DVKAADTYKD
710 720
GNIDAIDMAT LKKYLLGTIT QLPQG
Length:725
Mass (Da):79,776
Last modified:May 26, 2009 - v2
Checksum:i1C87FE4D03797C41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti609 – 6102TT → RR in AAA73868. (PubMed:1398087)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87018 Genomic DNA. Translation: AAA73868.1.
CP001348 Genomic DNA. Translation: ACL75110.1.
PIRiJC1300.
RefSeqiWP_015924277.1. NC_011898.1.
YP_002505090.1. NC_011898.1.

Genome annotation databases

EnsemblBacteriaiACL75110; ACL75110; Ccel_0731.
GeneIDi7309585.
KEGGicce:Ccel_0731.
PATRICi19432259. VBICloCel57783_0756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87018 Genomic DNA. Translation: AAA73868.1 .
CP001348 Genomic DNA. Translation: ACL75110.1 .
PIRi JC1300.
RefSeqi WP_015924277.1. NC_011898.1.
YP_002505090.1. NC_011898.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G87 X-ray 1.60 A/B 36-649 [» ]
1GA2 X-ray 1.70 A/B 36-649 [» ]
1K72 X-ray 1.80 A/B 36-649 [» ]
1KFG X-ray 1.90 A/B 36-649 [» ]
ProteinModelPortali P37700.
SMRi P37700. Positions 37-649.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 394503.Ccel_0731.

Protein family/group databases

CAZyi CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL75110 ; ACL75110 ; Ccel_0731 .
GeneIDi 7309585.
KEGGi cce:Ccel_0731.
PATRICi 19432259. VBICloCel57783_0756.

Phylogenomic databases

eggNOGi NOG05134.
HOGENOMi HOG000021032.
OMAi RKEVQFR.
OrthoDBi EOG6KQ6BP.

Enzyme and pathway databases

UniPathwayi UPA00696 .
BioCyci CCEL394503:GJET-752-MONOMER.

Miscellaneous databases

EvolutionaryTracei P37700.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.40.710. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR016134. Cellulos_enz_dockerin_1.
IPR018242. Dockerin_1.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view ]
Pfami PF00942. CBM_3. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
SMARTi SM01067. CBM_3. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS51172. CBM3. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum."
    Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., Belaich J.-P.
    Gene 119:17-28(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.

Entry informationi

Entry nameiGUNG_CLOCE
AccessioniPrimary (citable) accession number: P37700
Secondary accession number(s): B8I7V3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 26, 2009
Last modified: October 29, 2014
This is version 108 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3