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Protein

Endoglucanase E-4

Gene

celD

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 sitei427By similarity1
Active sitei461By similarity1
Active sitei470By 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

BRENDAi3.2.1.4. 6298.
UniPathwayiUPA00696.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase E-4 (EC:3.2.1.4)
Alternative name(s):
Cellulase E-4
Cellulase E4
Endo-1,4-beta-glucanase E-4
Gene namesi
Name:celD
OrganismiThermobifida fusca (Thermomonospora fusca)
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 461 PublicationAdd BLAST46
ChainiPRO_000000795947 – 880Endoglucanase E-4Add BLAST834

Interactioni

Protein-protein interaction databases

STRINGi269800.Tfu_2176.

Structurei

Secondary structure

1880
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi52 – 65Combined sources14
Turni85 – 88Combined sources4
Helixi89 – 91Combined sources3
Beta strandi102 – 104Combined sources3
Helixi109 – 125Combined sources17
Helixi127 – 132Combined sources6
Helixi136 – 152Combined sources17
Beta strandi159 – 165Combined sources7
Helixi167 – 172Combined sources6
Helixi177 – 179Combined sources3
Beta strandi186 – 190Combined sources5
Helixi196 – 213Combined sources18
Turni214 – 216Combined sources3
Helixi218 – 237Combined sources20
Helixi242 – 244Combined sources3
Helixi249 – 252Combined sources4
Helixi259 – 273Combined sources15
Helixi276 – 285Combined sources10
Helixi286 – 288Combined sources3
Beta strandi295 – 298Combined sources4
Beta strandi305 – 307Combined sources3
Helixi310 – 321Combined sources12
Helixi324 – 336Combined sources13
Turni337 – 339Combined sources3
Beta strandi358 – 360Combined sources3
Helixi361 – 378Combined sources18
Helixi382 – 400Combined sources19
Beta strandi413 – 416Combined sources4
Helixi424 – 427Combined sources4
Beta strandi430 – 432Combined sources3
Beta strandi436 – 439Combined sources4
Turni466 – 469Combined sources4
Helixi473 – 476Combined sources4
Helixi477 – 490Combined sources14
Beta strandi508 – 517Combined sources10
Beta strandi520 – 531Combined sources12
Beta strandi542 – 550Combined sources9
Helixi557 – 559Combined sources3
Beta strandi561 – 563Combined sources3
Beta strandi565 – 569Combined sources5
Beta strandi576 – 579Combined sources4
Beta strandi582 – 588Combined sources7
Beta strandi596 – 598Combined sources3
Turni599 – 602Combined sources4
Beta strandi603 – 611Combined sources9
Helixi618 – 620Combined sources3
Helixi622 – 624Combined sources3
Beta strandi637 – 641Combined sources5
Beta strandi644 – 648Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JS4X-ray2.00A/B47-651[»]
1TF4X-ray1.90A/B47-651[»]
3TF4X-ray2.20A/B47-651[»]
4TF4X-ray2.00A/B47-651[»]
ProteinModelPortaliP26221.
SMRiP26221.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26221.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini504 – 652CBM3PROSITE-ProRule annotationAdd BLAST149
Domaini678 – 770Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST93
Domaini771 – 880CBM2PROSITE-ProRule annotationAdd BLAST110

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation
Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
ENOG410XPC9. LUCA.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
2.60.40.290. 1 hit.
2.60.40.710. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR001956. CBD_3.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR003961. FN3_dom.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00942. CBM_3. 1 hit.
PF00041. fn3. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM01067. CBM_3. 1 hit.
SM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49384. SSF49384. 2 hits.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51172. CBM3. 1 hit.
PS50853. FN3. 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.

P26221-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVTEPPPRR RGRHSRARRF LTSLGATAAL TAGMLGVPLA TGTAHAEPAF
60 70 80 90 100
NYAEALQKSM FFYEAQRSGK LPENNRVSWR GDSGLNDGAD VGLDLTGGWY
110 120 130 140 150
DAGDHVKFGF PMAFTATMLA WGAIESPEGY IRSGQMPYLK DNLRWVNDYF
160 170 180 190 200
IKAHPSPNVL YVQVGDGDAD HKWWGPAEVM PMERPSFKVD PSCPGSDVAA
210 220 230 240 250
ETAAAMAASS IVFADDDPAY AATLVQHAKQ LYTFADTYRG VYSDCVPAGA
260 270 280 290 300
FYNSWSGYQD ELVWGAYWLY KATGDDSYLA KAEYEYDFLS TEQQTDLRSY
310 320 330 340 350
RWTIAWDDKS YGTYVLLAKE TGKQKYIDDA NRWLDYWTVG VNGQRVPYSP
360 370 380 390 400
GGMAVLDTWG ALRYAANTAF VALVYAKVID DPVRKQRYHD FAVRQINYAL
410 420 430 440 450
GDNPRNSSYV VGFGNNPPRN PHHRTAHGSW TDSIASPAEN RHVLYGALVG
460 470 480 490 500
GPGSPNDAYT DDRQDYVANE VATDYNAGFS SALAMLVEEY GGTPLADFPP
510 520 530 540 550
TEEPDGPEIF VEAQINTPGT TFTEIKAMIR NQSGWPARML DKGTFRYWFT
560 570 580 590 600
LDEGVDPADI TVSSAYNQCA TPEDVHHVSG DLYYVEIDCT GEKIFPGGQS
610 620 630 640 650
EHRREVQFRI AGGPGWDPSN DWSFQGIGNE LAPAPYIVLY DDGVPVWGTA
660 670 680 690 700
PEEGEEPGGG EGPGGGEEPG EDVTPPSAPG SPAVRDVTST SAVLTWSASS
710 720 730 740 750
DTGGSGVAGY DVFLRAGTGQ EQKVGSTTRT SFTLTGLEPD TTYIAAVVAR
760 770 780 790 800
DNAGNVSQRS TVSFTTLAEN GGGPDASCTV GYSTNDWDSG FTASIRITYH
810 820 830 840 850
GTAPLSSWEL SFTFPAGQQV THGWNATWRQ DGAAVTATPM SWNSSLAPGA
860 870 880
TVEVGFNGSW SGSNTPPTDF TLNGEPCALA
Length:880
Mass (Da):95,203
Last modified:November 1, 1997 - v2
Checksum:i5EA9A6ABF45A4D9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20093 Genomic DNA. Translation: AAB42155.1.
PIRiB42360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20093 Genomic DNA. Translation: AAB42155.1.
PIRiB42360.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JS4X-ray2.00A/B47-651[»]
1TF4X-ray1.90A/B47-651[»]
3TF4X-ray2.20A/B47-651[»]
4TF4X-ray2.00A/B47-651[»]
ProteinModelPortaliP26221.
SMRiP26221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269800.Tfu_2176.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
ENOG410XPC9. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00696.
BRENDAi3.2.1.4. 6298.

Miscellaneous databases

EvolutionaryTraceiP26221.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
2.60.40.290. 1 hit.
2.60.40.710. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR001956. CBD_3.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR003961. FN3_dom.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00942. CBM_3. 1 hit.
PF00041. fn3. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM01067. CBM_3. 1 hit.
SM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49384. SSF49384. 2 hits.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51172. CBM3. 1 hit.
PS50853. FN3. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN4_THEFU
AccessioniPrimary (citable) accession number: P26221
Secondary accession number(s): Q08167
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 119 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, Direct protein sequencing

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

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.