Cellulase Cel9-M - Clostridium cellulolyticum

Preferred order of sections

Names and origin

Protein names

Submitted name:
Cellulase Cel9-M EMBL AAG45160.1

Gene names

Name:

celM EMBL AAG45160.1

Organism

Clostridium cellulolyticum EMBL AAG45160.1

Taxonomic identifier

1521 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1IA7 PDB 1IA6 Metal-binding PDB 1IA7 PDB 1IA6 Nickel PDB 1IA7 PDB 1IA6 Zinc PDB 1IA7 PDB 1IA6
Technical term	3D-structure PDB 1IA7 PDB 1IA6
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

31

1

Nickel PDB 1IA7 PDB 1IA6

Metal binding

34

1

Nickel; via tele nitrogen PDB 1IA7 PDB 1IA6

Metal binding

52

1

Zinc PDB 1IA7 PDB 1IA6

Metal binding

68

1

Zinc PDB 1IA7 PDB 1IA6

Metal binding

69

1

Zinc; via pros nitrogen PDB 1IA7 PDB 1IA6

Metal binding

85

1

Zinc; via tele nitrogen PDB 1IA7 PDB 1IA6

Metal binding

238

1

Calcium PDB 1IA7 PDB 1IA6

Metal binding

241

1

Calcium PDB 1IA7 PDB 1IA6

Metal binding

242

1

Calcium PDB 1IA7 PDB 1IA6

Metal binding

287

1

Calcium; via carbonyl oxygen PDB 1IA7 PDB 1IA6

Metal binding

373

1

Nickel PDB 1IA7 PDB 1IA6

Sequences

Sequence

Length

Mass (Da)

Tools

Q9EYQ2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 526CDF064C5AAC9E
Show »

FASTA

526

57,631

        10         20         30         40         50         60 
MKSKLIKLSA IIISGVMLTT SFVNTGTAFA AGTHDYSTAL KDSIIFFDAN KCGPQAGENN 

        70         80         90        100        110        120 
VFDWRGACHT TDGSDVGVDL TGGYHDAGDH VKFGLPQGYS AAILGWSLYE FKESFDATGN 

       130        140        150        160        170        180 
TTKMLQQLKY FTDYFLKSHP NSTTFYYQVG EGNADHTYWG APEEQTGQRP SLYKADPSSP 

       190        200        210        220        230        240 
ASDILSETSA ALTLMYLNYK NIDSAYATKC LNAAKELYAM GKANQGVGNG QSFYQATSFG 

       250        260        270        280        290        300 
DDLAWAATWL YTATNDSTYI TDAEQFITLG NTMNENKMQD KWTMCWDDMY VPAALRLAQI 

       310        320        330        340        350        360 
TGKQIYKDAI EINFNYWKTQ VTTTPGGLKW LSNWGVLRYA AAESMVMLVY CKQNPDQSLL 

       370        380        390        400        410        420 
DLAKKQVDYI LGDNPANMSY IIGYGSNWCI HPHHRAANGY TYANGDNAKP AKHLLTGALV 

       430        440        450        460        470        480 
GGPDQNDKFL DDANQYQYTE VALDYNAGLV GVLAGAIKFF GGTIVNPPVK KGDLNNDTFI 

       490        500        510        520 
DAIDLALCKN YILTQNGNID KNNADMNGDG SIDAIDFSLL KKAILG

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References

[1]	"Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome." Belaich A., Parsiegla G., Gal L., Villard C., Haser R., Belaich J.P. J. Bacteriol. 184:1378-1384(2002) [PubMed: 11844767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases." Parsiegla G., Belaich A., Belaich J.P., Haser R. Biochemistry 41:11134-11142(2002) [PubMed: 12220178] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 31-471 IN COMPLEX WITH CALCIUM; NICKEL AND ZINC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF316823 Genomic DNA. Translation: AAG45160.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IA6	X-ray	1.80	A	31-471	[»]
1IA7	X-ray	2.00	A	31-471	[»]

ProteinModelPortal

Q9EYQ2.

SMR

Q9EYQ2. Positions 31-461.

ModBase

Search...

Protein family/group databases

CAZy

GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]

Gene3D

G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.

Pfam

PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]

SUPFAM

SSF63446. Cellulos_enz_dockerin_1. 1 hit.
SSF48208. Glyco_trans_6hp. 1 hit.

PROSITE

PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9EYQ2_9CLOT

Accession

Primary (citable) accession number: Q9EYQ2

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2001
Last sequence update:	March 1, 2001
Last modified:	September 21, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)