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Protein

Major extracellular endoglucanase

Gene

engXCA

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei182Proton 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:
Major extracellular endoglucanase (EC:3.2.1.4)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:engXCA
Ordered Locus Names:XCC3521
OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Taxonomic identifieri190485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
Proteomesi
  • UP000001010 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000000787526 – 484Major extracellular endoglucanaseAdd BLAST459

Interactioni

Protein-protein interaction databases

STRINGi190485.XCC3521.

Structurei

Secondary structure

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi45 – 48Combined sources4
Turni60 – 64Combined sources5
Helixi67 – 76Combined sources10
Beta strandi81 – 86Combined sources6
Helixi88 – 91Combined sources4
Turni102 – 104Combined sources3
Helixi106 – 108Combined sources3
Helixi113 – 127Combined sources15
Beta strandi130 – 135Combined sources6
Beta strandi138 – 142Combined sources5
Beta strandi145 – 147Combined sources3
Helixi154 – 168Combined sources15
Beta strandi174 – 178Combined sources5
Beta strandi188 – 192Combined sources5
Turni194 – 196Combined sources3
Helixi198 – 212Combined sources15
Beta strandi216 – 220Combined sources5
Beta strandi227 – 229Combined sources3
Helixi242 – 245Combined sources4
Turni253 – 255Combined sources3
Beta strandi256 – 258Combined sources3
Beta strandi261 – 263Combined sources3
Turni265 – 267Combined sources3
Helixi271 – 274Combined sources4
Turni278 – 281Combined sources4
Helixi282 – 289Combined sources8
Helixi291 – 293Combined sources3
Turni294 – 296Combined sources3
Beta strandi301 – 305Combined sources5
Helixi313 – 328Combined sources16
Beta strandi334 – 337Combined sources4
Beta strandi339 – 341Combined sources3
Turni344 – 346Combined sources3
Helixi359 – 369Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TUFX-ray2.70A/B/C/D26-371[»]
ProteinModelPortaliP19487.
SMRiP19487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini395 – 484CBM2PROSITE-ProRule annotationAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni375 – 399Thr-Pro repeats ("hinge") (Pro-Thr box)Add BLAST25

Domaini

The C-terminal region of the protein is not crucial for activity.
The Thr/Pro-rich region (also termed "hinge") may be a potential site for proteolysis.

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4106R7G. Bacteria.
COG2730. LUCA.
COG5297. LUCA.
HOGENOMiHOG000225207.
KOiK01179.
OMAiGTVNNLW.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
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.

P19487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIFRTASTL ALATALALAA GPAFSYSINN SRQIVDDSGK VVQLKGVNVF
60 70 80 90 100
GFETGNHVMH GLWARNWKDM IVQMQGLGFN AVRLPFCPAT LRSDTMPASI
110 120 130 140 150
DYSRNADLQG LTSLQILDKV IAEFNARGMY VLLDHHTPDC AGISELWYTG
160 170 180 190 200
SYTEAQWLAD LRFVANRYKN VPYVLGLDLK NEPHGAATWG TGNAATDWNK
210 220 230 240 250
AAERGSAAVL AVAPKWLIAV EGITDNPVCS TNGGIFWGGN LQPLACTPLN
260 270 280 290 300
IPANRLLLAP HVYGPDVFVQ SYFNDSNFPN NMPAIWERHF GQFAGTHALL
310 320 330 340 350
LGEFGGKYGE GDARDKTWQD ALVKYLRSKG INQGFYWSWN PNSGDTGGIL
360 370 380 390 400
RDDWTSVRQD KMTLLRTLWG TAGNTTPTPT PTPTPTPTPT PTPTPTPTPG
410 420 430 440 450
TSTFSTKVIV DNSWNGGYCN RVQVTNTGTA SGTWSIAVPV TGTVNNAWNA
460 470 480
TWSQSGSTLR ASGVDFNRTL AAGATAEFGF CAAS
Length:484
Mass (Da):52,242
Last modified:July 11, 2002 - v2
Checksum:i6671AE5BF1B7602A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti410 – 484VDNSW…FCAAS → ASPVVGSAARKLPAASRLAC HWPASSTGWRVWVIAAPSVT WKRPHAARAIERRMRVTRLR RATRLNRGPLPAPAHTTQHA PRL in AAA27612 (PubMed:2373365).CuratedAdd BLAST75

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32700 Genomic DNA. Translation: AAA27612.1.
AE008922 Genomic DNA. Translation: AAM42791.1.
PIRiJH0158.
RefSeqiNP_638867.1. NC_003902.1.
WP_011038613.1. NC_003902.1.

Genome annotation databases

EnsemblBacteriaiAAM42791; AAM42791; XCC3521.
GeneIDi1000085.
KEGGixcc:XCC3521.
PATRICi24078160. VBIXanCam115730_3766.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32700 Genomic DNA. Translation: AAA27612.1.
AE008922 Genomic DNA. Translation: AAM42791.1.
PIRiJH0158.
RefSeqiNP_638867.1. NC_003902.1.
WP_011038613.1. NC_003902.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TUFX-ray2.70A/B/C/D26-371[»]
ProteinModelPortaliP19487.
SMRiP19487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190485.XCC3521.

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

EnsemblBacteriaiAAM42791; AAM42791; XCC3521.
GeneIDi1000085.
KEGGixcc:XCC3521.
PATRICi24078160. VBIXanCam115730_3766.

Phylogenomic databases

eggNOGiENOG4106R7G. Bacteria.
COG2730. LUCA.
COG5297. LUCA.
HOGENOMiHOG000225207.
KOiK01179.
OMAiGTVNNLW.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiGUNA_XANCP
AccessioniPrimary (citable) accession number: P19487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: November 2, 2016
This is version 122 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.