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P19487 (GUNA_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major extracellular endoglucanase

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:engXCA
Ordered Locus Names:XCC3521
OrganismXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]
Taxonomic identifier190485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Domain

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 similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.1
Chain26 – 484459Major extracellular endoglucanase
PRO_0000007875

Regions

Region375 – 39925Thr-Pro repeats ("hinge") (Pro-Thr box)

Sites

Active site1821Proton donor By similarity
Active site3031Nucleophile By similarity

Experimental info

Sequence conflict410 – 48475VDNSW…FCAAS → ASPVVGSAARKLPAASRLAC HWPASSTGWRVWVIAAPSVT WKRPHAARAIERRMRVTRLR RATRLNRGPLPAPAHTTQHA PRL in AAA27612. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19487 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 6671AE5BF1B7602A

FASTA48452,242
        10         20         30         40         50         60 
MSIFRTASTL ALATALALAA GPAFSYSINN SRQIVDDSGK VVQLKGVNVF GFETGNHVMH 

        70         80         90        100        110        120 
GLWARNWKDM IVQMQGLGFN AVRLPFCPAT LRSDTMPASI DYSRNADLQG LTSLQILDKV 

       130        140        150        160        170        180 
IAEFNARGMY VLLDHHTPDC AGISELWYTG SYTEAQWLAD LRFVANRYKN VPYVLGLDLK 

       190        200        210        220        230        240 
NEPHGAATWG TGNAATDWNK AAERGSAAVL AVAPKWLIAV EGITDNPVCS TNGGIFWGGN 

       250        260        270        280        290        300 
LQPLACTPLN IPANRLLLAP HVYGPDVFVQ SYFNDSNFPN NMPAIWERHF GQFAGTHALL 

       310        320        330        340        350        360 
LGEFGGKYGE GDARDKTWQD ALVKYLRSKG INQGFYWSWN PNSGDTGGIL RDDWTSVRQD 

       370        380        390        400        410        420 
KMTLLRTLWG TAGNTTPTPT PTPTPTPTPT PTPTPTPTPG TSTFSTKVIV DNSWNGGYCN 

       430        440        450        460        470        480 
RVQVTNTGTA SGTWSIAVPV TGTVNNAWNA TWSQSGSTLR ASGVDFNRTL AAGATAEFGF 


CAAS 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the engXCA gene encoding the major endoglucanase of Xanthomonas campestris pv. campestris."
Gough C.L., Dow J.M., Keen J., Henrissat B., Daniels M.J.
Gene 89:53-59(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-61.
[2]"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. expand/collapse author list , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32700 Genomic DNA. Translation: AAA27612.1.
AE008922 Genomic DNA. Translation: AAM42791.1.
PIRJH0158.
RefSeqNP_638867.1. NC_003902.1.

3D structure databases

ProteinModelPortalP19487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190485.XCC3521.

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM42791; AAM42791; XCC3521.
GeneID1000085.
KEGGxcc:XCC3521.
PATRIC24078160. VBIXanCam115730_3766.

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000225207.
KOK01179.
OMAWIVAVEG.
OrthoDBEOG6FRCSN.
ProtClustDBCLSK636809.

Enzyme and pathway databases

BioCycXCAM190485:GIXZ-3519-MONOMER.

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. 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]
PfamPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNA_XANCP
AccessionPrimary (citable) accession number: P19487
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: November 13, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries