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P27033

- GUNC_CELJU

UniProt

P27033 - GUNC_CELJU

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Protein

Endoglucanase C

Gene

celC

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed - Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei502 – 5021Proton donorBy similarity
Active sitei652 – 6521NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose 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

BioCyciCJAP498211:GHIT-1456-MONOMER.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase C (EC:3.2.1.4)
Alternative name(s):
Cellodextrinase C
Cellulase C
Endo-1,4-beta-glucanase C
Short name:
EGC
Gene namesi
Name:celC
Synonyms:cel5A
Ordered Locus Names:CJA_1462
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
ProteomesiUP000001036: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 747710Endoglucanase CPRO_0000007865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 133By similarity
Disulfide bondi183 ↔ 214By similarity
Disulfide bondi193 ↔ 208By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_1462.

Structurei

3D structure databases

ProteinModelPortaliP27033.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 13699CBM2Add
BLAST
Domaini182 – 20928CBM10Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 747468CatalyticAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi137 – 17943Ser-rich (linker)Add
BLAST
Compositional biasi227 – 27953Ser-rich (linker)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000066200.
OMAiRTIQQTM.
OrthoDBiEOG6PS5R7.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
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]
PfamiPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 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.

P27033-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGHVTSPSKR YPASFKRAGS ILGVSIALAA FSNVAAAGCE YVVTNSWGSG
60 70 80 90 100
FTAAIRITNS TSSVINGWNV SWQYNSNRVT NLWNANLSGS NPYSASNLSW
110 120 130 140 150
NGTIQPGQTV EFGFQGVTNS GTVESPTVNG AACTGGTSSS VSSSSVVSSS
160 170 180 190 200
SSSRSSVSSS SVVSSSSSVV SSSSSSVVSG GQCNWYGTLY PLCVSTTSGW
210 220 230 240 250
GYENNRSCIS PSTCSAQPAP YGIVGGSSSP SSISSSSVRS SSSSSVVPPS
260 270 280 290 300
SSSSSSVPSS SSSSVSSSSV VSSSSSSVSV PGTGVFRVNT QGNLTKDGQL
310 320 330 340 350
LPARCGNWFG LEGRHEPSND ADNPSGAPME LYAGNMWWVN NSQGSGRTIQ
360 370 380 390 400
QTMTELKQQG ITMLRLPIAP QTLDANDPQG RSPNLKNHQS IRQSNARQAL
410 420 430 440 450
EDFIKLADQN DIQIFIDIHS CSNYVGWRAG RLDARPPYVD ANRVGYDFTR
460 470 480 490 500
EEYSCSATNN PSSVTRIHAY DKQKWLANLR EIAGLSAKLG VSNLIGIDVF
510 520 530 540 550
NEPYDYTWAE WKGMVEEAYQ AINEVNPNML IIVEGISANA NTQDGTPDTS
560 570 580 590 600
VPVPHGSTDL NPNWGENLYE AGANPPNIPK DRLLFSPHTY GPSVFVQRQF
610 620 630 640 650
MDPAQTECAG LEGDEAAQAR CRIVINPTVL EQGWEEHFGY LRELGYGILI
660 670 680 690 700
GEFGGNMDWP GAKSSQADRN AWSHITTNVD QQWQQAAASY FKRKGINACY
710 720 730 740
WSMNPESADT MGWYLTPWDP VTANDMWGQW TGFDPRKTQL LHNMWGL
Length:747
Mass (Da):80,098
Last modified:April 20, 2010 - v2
Checksum:i2A1D90E2612D361A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851A → P in CAA43597. (PubMed:1953673)Curated
Sequence conflicti181 – 1811G → GG in CAA43597. (PubMed:1953673)Curated
Sequence conflicti262 – 2621S → C in CAA43597. (PubMed:1953673)Curated
Sequence conflicti291 – 2911Q → K in CAA43597. (PubMed:1953673)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61299 Genomic DNA. Translation: CAA43597.1.
CP000934 Genomic DNA. Translation: ACE82870.1.
PIRiS19652.
RefSeqiYP_001981949.1. NC_010995.1.

Genome annotation databases

EnsemblBacteriaiACE82870; ACE82870; CJA_1462.
GeneIDi6413622.
KEGGicja:CJA_1462.
PATRICi21326306. VBICelJap122165_1442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61299 Genomic DNA. Translation: CAA43597.1 .
CP000934 Genomic DNA. Translation: ACE82870.1 .
PIRi S19652.
RefSeqi YP_001981949.1. NC_010995.1.

3D structure databases

ProteinModelPortali P27033.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 498211.CJA_1462.

Protein family/group databases

CAZyi CBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACE82870 ; ACE82870 ; CJA_1462 .
GeneIDi 6413622.
KEGGi cja:CJA_1462.
PATRICi 21326306. VBICelJap122165_1442.

Phylogenomic databases

HOGENOMi HOG000066200.
OMAi RTIQQTM.
OrthoDBi EOG6PS5R7.

Enzyme and pathway databases

BioCyci CJAP498211:GHIT-1456-MONOMER.

Family and domain databases

Gene3Di 2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
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 PF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM00637. CBD_II. 1 hit.
SM01064. CBM_10. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF57615. SSF57615. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The cellodextrinase from Pseudomonas fluorescens subsp. cellulosa consists of multiple functional domains."
    Ferreira L.M.A., Hazlewood G.P., Barker P.J., Gilbert H.J.
    Biochem. J. 279:793-799(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-47.
  2. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
    DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
    J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ueda107.

Entry informationi

Entry nameiGUNC_CELJU
AccessioniPrimary (citable) accession number: P27033
Secondary accession number(s): B3PDK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: April 20, 2010
Last modified: October 1, 2014
This is version 104 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3