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Protein

Endoglucanase D

Gene

engD

Organism
Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Has endoglucanase activity on carboxymethyl-cellulose (CMC), cellobiosidase activity on p-nitrophenyl-cellobioside (p-NPC), and partial hydrolytic activity on crystalline cellulose (Avicel).

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei180Proton donorBy similarity1
Active sitei303NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase D (EC:3.2.1.4)
Alternative name(s):
Cellulase D
Endo-1,4-beta-glucanase D
Gene namesi
Name:engD
Ordered Locus Names:Clocel_3242
OrganismiClostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)
Taxonomic identifieri573061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000002730 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 311 PublicationAdd BLAST31
ChainiPRO_000000784832 – 515Endoglucanase DAdd BLAST484

Interactioni

Protein-protein interaction databases

STRINGi573061.Clocel_3242.

Structurei

Secondary structure

1515
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 50Combined sources8
Beta strandi52 – 56Combined sources5
Turni57 – 61Combined sources5
Turni66 – 69Combined sources4
Helixi76 – 85Combined sources10
Beta strandi89 – 92Combined sources4
Turni103 – 105Combined sources3
Helixi110 – 124Combined sources15
Turni125 – 127Combined sources3
Beta strandi129 – 132Combined sources4
Turni138 – 140Combined sources3
Turni145 – 147Combined sources3
Helixi148 – 165Combined sources18
Turni166 – 168Combined sources3
Beta strandi173 – 177Combined sources5
Helixi186 – 188Combined sources3
Helixi195 – 214Combined sources20
Helixi217 – 220Combined sources4
Beta strandi224 – 227Combined sources4
Helixi229 – 231Combined sources3
Helixi235 – 240Combined sources6
Helixi244 – 246Combined sources3
Beta strandi250 – 255Combined sources6
Helixi260 – 263Combined sources4
Helixi275 – 291Combined sources17
Helixi293 – 295Combined sources3
Beta strandi299 – 304Combined sources6
Helixi312 – 327Combined sources16
Turni328 – 330Combined sources3
Beta strandi332 – 337Combined sources6
Turni354 – 357Combined sources4
Beta strandi358 – 361Combined sources4
Helixi362 – 372Combined sources11
Beta strandi411 – 420Combined sources10
Beta strandi422 – 433Combined sources12
Beta strandi435 – 437Combined sources3
Beta strandi439 – 441Combined sources3
Beta strandi443 – 447Combined sources5
Beta strandi452 – 465Combined sources14
Beta strandi468 – 473Combined sources6
Turni482 – 484Combined sources3
Beta strandi485 – 495Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NDYX-ray2.10A/B/C/D32-376[»]
E/F/G/H409-515[»]
3NDZX-ray2.08A/B/C/D32-376[»]
E/F/G/H409-515[»]
ProteinModelPortaliP28623.
SMRiP28623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28623.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini404 – 515CBM2PROSITE-ProRule annotationAdd BLAST112

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 376CatalyticBy similarityAdd BLAST345

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi377 – 407Pro/Thr-rich (linker)Add BLAST31

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108K2F. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000027405.
KOiK01179.
OMAiPEDEHIG.
OrthoDBiPOG091H14IK.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
PROSITEiPS51173. CBM2. 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.

P28623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKHLLSRGK LLLFVSVMAT SSIIAGGNAY GSTAFTGVRD VPAQQIVNEM
60 70 80 90 100
KVGWNLGNTM DAIGGETNWG NPMTTHAMIN KIKEAGFNTL RLPVTWDGHM
110 120 130 140 150
GAAPEYTIDQ TWMKRVEEIA NYAFDNDMYV IINLHHENEW LKPFYANEAQ
160 170 180 190 200
VKAQLTKVWT QIANNFKKYG DHLIFETMNE PRPVGASNEW TGGSYENREV
210 220 230 240 250
VNRYNLTAVN AIRATGGNNA TRYIMVPTLA ASAMSTTIND LVIPNNDSKV
260 270 280 290 300
IVSLHMYSPY FFAMDINGTS SWGSDYDKSS LDSEFDAVYN KFVKNGRAVV
310 320 330 340 350
IGEMGSINKN NTAARVTHAE YYAKSAKARG LTPIWWDNGY SVAGKAETFG
360 370 380 390 400
IFNRSNLTWD APEVMKAFIK GIGGSSTTTP TTPTTPTTPT TPTTPTTPTT
410 420 430 440 450
PTTPTTPQSA VEVTYAITNS WGSGASVNVT IKNNGTTPIN GWTLKWTMPI
460 470 480 490 500
NQTITNMWSA SFVASGTTLS VTNAGYNGTI AANGGTQSFG FNINYSGVLS
510
KPTGFTVNGT ECTVK
Length:515
Mass (Da):55,978
Last modified:November 30, 2010 - v2
Checksum:i57F15B035856008E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti188 – 189NE → LQ in AAA23233 (PubMed:1538700).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37434 Genomic DNA. Translation: AAA23233.1.
CP002160 Genomic DNA. Translation: ADL52928.1.
PIRiS20493.
RefSeqiWP_010073314.1. NC_014393.1.

Genome annotation databases

EnsemblBacteriaiADL52928; ADL52928; Clocel_3242.
KEGGiccb:Clocel_3242.
PATRICi41732687. VBICloCel81632203721_0262.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37434 Genomic DNA. Translation: AAA23233.1.
CP002160 Genomic DNA. Translation: ADL52928.1.
PIRiS20493.
RefSeqiWP_010073314.1. NC_014393.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NDYX-ray2.10A/B/C/D32-376[»]
E/F/G/H409-515[»]
3NDZX-ray2.08A/B/C/D32-376[»]
E/F/G/H409-515[»]
ProteinModelPortaliP28623.
SMRiP28623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi573061.Clocel_3242.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL52928; ADL52928; Clocel_3242.
KEGGiccb:Clocel_3242.
PATRICi41732687. VBICloCel81632203721_0262.

Phylogenomic databases

eggNOGiENOG4108K2F. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000027405.
KOiK01179.
OMAiPEDEHIG.
OrthoDBiPOG091H14IK.

Miscellaneous databases

EvolutionaryTraceiP28623.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
PROSITEiPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUND_CLOC7
AccessioniPrimary (citable) accession number: P28623
Secondary accession number(s): D9SUH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 30, 2010
Last modified: November 30, 2016
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, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.