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P28623

- GUND_CLOC7

UniProt

P28623 - GUND_CLOC7

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Protein

Endoglucanase D

Gene

engD

Organism
Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei180 – 1801Proton donorBy similarity
Active sitei303 – 3031NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCCEL573061:GIXD-3329-MONOMER.

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
ProteomesiUP000002730: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 515484Endoglucanase DPRO_0000007848Add
BLAST

Structurei

Secondary structure

1
515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 508Combined sources
Beta strandi52 – 565Combined sources
Turni57 – 615Combined sources
Turni66 – 694Combined sources
Helixi76 – 8510Combined sources
Beta strandi89 – 924Combined sources
Turni103 – 1053Combined sources
Helixi110 – 12415Combined sources
Turni125 – 1273Combined sources
Beta strandi129 – 1324Combined sources
Turni138 – 1403Combined sources
Turni145 – 1473Combined sources
Helixi148 – 16518Combined sources
Turni166 – 1683Combined sources
Beta strandi173 – 1775Combined sources
Helixi186 – 1883Combined sources
Helixi195 – 21420Combined sources
Helixi217 – 2204Combined sources
Beta strandi224 – 2274Combined sources
Helixi229 – 2313Combined sources
Helixi235 – 2406Combined sources
Helixi244 – 2463Combined sources
Beta strandi250 – 2556Combined sources
Helixi260 – 2634Combined sources
Helixi275 – 29117Combined sources
Helixi293 – 2953Combined sources
Beta strandi299 – 3046Combined sources
Helixi312 – 32716Combined sources
Turni328 – 3303Combined sources
Beta strandi332 – 3376Combined sources
Turni354 – 3574Combined sources
Beta strandi358 – 3614Combined sources
Helixi362 – 37211Combined sources
Beta strandi411 – 42010Combined sources
Beta strandi422 – 43312Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi439 – 4413Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi452 – 46514Combined sources
Beta strandi468 – 4736Combined sources
Turni482 – 4843Combined sources
Beta strandi485 – 49511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28623.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini404 – 515112CBM2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 376345CatalyticBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi377 – 40731Pro/Thr-rich (linker)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000027405.
KOiK01179.
OMAiACINDYN.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1892NE → LQ in AAA23233. (PubMed:1538700)Curated

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. NZ_BABR01000032.1.
YP_003844692.1. NC_014393.1.

Genome annotation databases

EnsemblBacteriaiADL52928; ADL52928; Clocel_3242.
GeneIDi9610136.
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 .
PIRi S20493.
RefSeqi WP_010073314.1. NZ_BABR01000032.1.
YP_003844692.1. NC_014393.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NDY X-ray 2.10 A/B/C/D 32-376 [» ]
E/F/G/H 409-515 [» ]
3NDZ X-ray 2.08 A/B/C/D 32-376 [» ]
E/F/G/H 409-515 [» ]
ProteinModelPortali P28623.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADL52928 ; ADL52928 ; Clocel_3242 .
GeneIDi 9610136.
KEGGi ccb:Clocel_3242.
PATRICi 41732687. VBICloCel81632203721_0262.

Phylogenomic databases

HOGENOMi HOG000027405.
KOi K01179.
OMAi ACINDYN.

Enzyme and pathway databases

BioCyci CCEL573061:GIXD-3329-MONOMER.

Miscellaneous databases

EvolutionaryTracei P28623.

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM00637. CBD_II. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of functional domains of endoglucanases from Clostridium cellulovorans by gene cloning, nucleotide sequencing and chimeric protein construction."
    Hamamoto T., Foong F., Shoseyov O., Doi R.H.
    Mol. Gen. Genet. 231:472-479(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-44.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35296 / DSM 3052 / OCM 3 / 743B.

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 26, 2014
This is version 96 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

External Data

Dasty 3