Endoglucanase C precursor - Cellulomonas fimi

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Reviewed, UniProtKB/Swiss-Prot P14090 (GUNC_CELFI)

Last modified June 16, 2009. Version 90. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Endoglucanase C
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase C
    Cellulase C

Gene names

Name:

cenC

Organism

Cellulomonas fimi

Taxonomic identifier

1708 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

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Protein attributes

Sequence length	1101 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Contains 2 CBM-cenC (cenC-type cellulose-binding) domains.

Contains 2 Ig-like (immunoglobulin-like) domains.

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Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Immunoglobulin domain Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

Ref.1

Chain

33 – 1101

1069

Endoglucanase C

PRO_0000007946

Regions

Domain

64 – 173

110

CBM-cenC 1

Domain

212 – 318

107

CBM-cenC 2

Domain

918 – 1006

Ig-like 1

Domain

1008 – 1097

Ig-like 2

Region

329 – 880

552

Catalytic

Sites

Active site

831

By similarity

Active site

882

By similarity

Active site

891

By similarity

Secondary structure

1101

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P14090-1 [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: 1FBAD189CC5F8B5D
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FASTA

1,101

115,216

        10         20         30         40         50         60 
MVSRRSSQAR GALTAVVATL ALALAGSGTA LAASPIGEGT FDDGPEGWVA YGTDGPLDTS 

        70         80         90        100        110        120 
TGALCVAVPA GSAQYGVGVV LNGVAIEEGT TYTLRYTATA STDVTVRALV GQNGAPYGTV 

       130        140        150        160        170        180 
LDTSPALTSE PRQVTETFTA SATYPATPAA DDPEGQIAFQ LGGFSADAWT FCLDDVALDS 

       190        200        210        220        230        240 
EVELLPHTSF AESLGPWSLY GTSEPVFADG RMCVDLPGGQ GNPWDAGLVY NGVPVGEGES 

       250        260        270        280        290        300 
YVLSFTASAT PDMPVRVLVG EGGGAYRTAF EQGSAPLTGE PATREYAFTS NLTFPPDGDA 

       310        320        330        340        350        360 
PGQVAFHLGK AGAYEFCISQ VSLTTSATPP PGYEPDTGPR VRVNQVGYLP FGPKRATLVT 

       370        380        390        400        410        420 
DAAEPVAWEL RDADGVVVAD GTSEPRGVEP SAAQAVHVLD FSDVTTQGAG YTLVADGETS 

       430        440        450        460        470        480 
RPFDIDGDLY QQLRYDALNY FYLARSGTEI EADVVGEEYA REAGHVGVAP NQGDTDVPCI 

       490        500        510        520        530        540 
GPRDYYDGWT CDYRLDVSGG WYDAGDHGKY VVNGGIAVGQ LLQTYERALH AGTADALADG 

       550        560        570        580        590        600 
TLDVPEHGND VPDVLDEARW ELEWMLSMIV PEGEYAGMVH HKVHDEGWTG LPLLPADDPQ 

       610        620        630        640        650        660 
ARSLHRPSTA ATLNLSAVAA QGARLLEPYD PQLAQTLLEA ARTTWAAAQE HPALYAPGEA 

       670        680        690        700        710        720 
GADGGGAYND SQVADEFYWA AAELYLTTGE DAFATAVTTS PLHTADVFTA DGFGWGSVAA 

       730        740        750        760        770        780 
LGRLDLATVP NELPGLDAVQ SSVVEGAQEY LAAQAGQGFG SLYSPPGGEY VWGSSSQVAN 

       790        800        810        820        830        840 
NLVVVATAYD LTGDERFRAA TLEGLDYLFG RNALNQSYVT GWGEVASHQQ HSRWFAHQLD 

       850        860        870        880        890        900 
PSLPSPPPGS LAGGPNSQAA TWDPTTKAAF PDGCAPSACY VDEIQAWSTN ELTVNWNSAL 

       910        920        930        940        950        960 
SWVASWVADQ GSAEPVPTAP VVTRQPVDAT VALGADATFT AEASGVPAPT VRWQVRAGRG 

       970        980        990       1000       1010       1020 
WKDVAGATGT TLTVRATART DGTRYRAVFT NAAGSVESAV VRLTVERAAP VVTQHPADVR 

      1030       1040       1050       1060       1070       1080 
ARVGTRAVFR AAADGYPTPC VVWQVRWGGG SWRPIPWATS TTLSVPVTVL AAGTEYRAVF 

      1090       1100 
TNAVGTAATE PAELAVQRPR S

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References

[1]	"Nucleotide sequence of the endoglucanase C gene (cenC) of Cellulomonas fimi, its high-level expression in Escherichia coli, and characterization of its products." Coutinho J.B., Moser B., Kilburn D.G., Warren R.A.J., Miller R.C. Jr. Mol. Microbiol. 5:1221-1233(1991) [PubMed: 1956299] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-42. Strain: ATCC 484 / DSM 20113 / IFO 15513 / JCM 1341 / NCTC 7547.
[2]	"Purification and characterization of endoglucanase C of Cellulomonas fimi, cloning of the gene, and analysis of in vivo transcripts of the gene." Moser B., Gilkes N.R., Kilburn D.G., Warren R.A.J., Miller R.C. Jr. Appl. Environ. Microbiol. 55:2480-2487(1989) [PubMed: 2604391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64, PROTEIN SEQUENCE OF 625-641.
[3]	"The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats." Coutinho J.B., Gilkes N.R., Warren R.A.J., Kilburn D.G., Miller R.C. Jr. Mol. Microbiol. 6:1243-1252(1992) [PubMed: 1375311] [Abstract] Cited for: DOMAINS CELLULOSE BINDING.
[4]	"Members of the immunoglobulin superfamily in bacteria." Bateman A., Eddy S.R., Chothia C. Protein Sci. 5:1939-1942(1996) [PubMed: 8880921] [Abstract] Cited for: DOMAINS IG-LIKE.
[5]	"Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy." Johnson P.E., Joshi M.D., Tomme P., Kilburn D.G., McIntosh L.P. Biochemistry 35:14381-14394(1996) [PubMed: 8916925] [Abstract] Cited for: STRUCTURE BY NMR OF 33-184.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X57858 Genomic DNA. Translation: CAA40993.1.
M29707 Genomic DNA. Translation: AAA23087.1. Different termination.
M29708 Genomic DNA. Translation: AAA23088.1. Sequence problems.

PIR

S15271.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CX1	NMR	-	A	178-328	[»]
1GU3	X-ray	2.30	A	33-181	[»]
1ULO	NMR	-	A	33-184	[»]
1ULP	NMR	-	A	33-184	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Enzyme and pathway databases

BRENDA

3.2.1.4. 97800.

Family and domain databases

InterPro

IPR012341. 6hp_glycosidase.
IPR003305. CenC_carb_bd.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
[Graphical view]

Gene3D

G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

PANTHER

PTHR22298:SF3. Glyco_hydro_9. 1 hit.

Pfam

PF02018. CBM_4_9. 2 hits.
PF02927. CelD_N. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
PF07679. I-set. 2 hits.
[Graphical view]

SMART

SM00409. IG. 1 hit.
[Graphical view]

PROSITE

PS00592. GLYCOSYL_HYDROL_F9_1. False negative.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

GUNC_CELFI

Accession

Primary (citable) accession number: P14090

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families