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Protein

Endoglucanase D

Gene

cenD

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei208Proton donorBy similarity1
Active sitei349NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

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:cenD
OrganismiCellulomonas fimi
Taxonomic identifieri1708 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
ChainiPRO_000000784340 – 747Endoglucanase DAdd BLAST708

Interactioni

Protein-protein interaction databases

STRINGi590998.Celf_1924.

Structurei

3D structure databases

ProteinModelPortaliP50400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini456 – 543Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST88
Domaini552 – 639Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST88
Domaini638 – 747CBM2PROSITE-ProRule annotationAdd BLAST110

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4106R7G. Bacteria.
COG2730. LUCA.
COG3979. LUCA.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 2 hits.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR003961. FN3_dom.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
PF00041. fn3. 2 hits.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS50853. FN3. 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.

P50400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSASRTRAR TRVRTAVSGL LAATVLAAPL TLVAAPAQAA TGDDWLHVEG
60 70 80 90 100
NTIVDSTGKE AILSGVNWFG FNASERVFHG LWSGNITQIT QQMAQRGINV
110 120 130 140 150
VRVPVSTQLL LEWKAGTFLK PNVNTYANPE LEGKNSLQIF EYWLTLCQKY
160 170 180 190 200
GIKVFLDVHS AEADNSGHVY NMWWKGDITT EDVYEGWEWA ATRWKDDDTI
210 220 230 240 250
VGADIKNEPH GTQGSTERAK WDGTTDKDNF KHFAETASKK ILAINPNWLV
260 270 280 290 300
FVEGVEIYPK PGVPWTSTGL TDYYGTWWGG NLRGVRDHPI DLGAHQDQLV
310 320 330 340 350
YSPHDYGPLV FDQKWFQKDF DKASLTADVW GPNWLFIHDE DIAPLLIGEW
360 370 380 390 400
GGRLGQDPRQ DKWMAALRDL VAERRLSQTF WVLNPNSGDT GGLLLDDWKT
410 420 430 440 450
WDEVKYSTML EPTLWKHGGK YVGLDHQVPL GGVGSTTGTS ISQVGGGTPD
460 470 480 490 500
TTAPTAPTGL RAGTPTASTV PLTWSASTDT GGSGVAGYEV YRGTTLVGTT
510 520 530 540 550
TATSYTVTGL AADSAYTFSV RAKDGAGNTS AASAAVTART AAGGGDVTAP
560 570 580 590 600
SVPTGLTAGT PTATSVPLTW TASTDTGGSG VTGYEVYRGS TLVARPTGTS
610 620 630 640 650
HTVTGLSAAT AYTFTVRAVD AAGNVSAASA PVGVTTAPDP TTGSCAVTYT
660 670 680 690 700
ANGWSGGFTA AVTLTNTGTT ALSGWTLGFA FPSGQTLTQG WSARWAQSGS
710 720 730 740
SVTATNEAWN AVLAPGASVE IGFSGTHTGT NTAPATFTVG GATCTTR
Length:747
Mass (Da):78,937
Last modified:October 1, 1996 - v1
Checksum:iBD15473C9D8B42BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02544 Genomic DNA. Translation: AAA23089.1.
PIRiB47093.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02544 Genomic DNA. Translation: AAA23089.1.
PIRiB47093.

3D structure databases

ProteinModelPortaliP50400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi590998.Celf_1924.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4106R7G. Bacteria.
COG2730. LUCA.
COG3979. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00696.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 2 hits.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR003961. FN3_dom.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
PF00041. fn3. 2 hits.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS50853. FN3. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUND_CELFI
AccessioniPrimary (citable) accession number: P50400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.