DB code: D00535

CATH domain 2.60.120.200 : Jelly Rolls Catalytic domain
2.60.40.- : Immunoglobulin-like
E.C. 3.2.1.83
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.60.120.200 : Jelly Rolls S00148 D00666 M00185 S00511 T00064 T00208

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
P43478 Kappa-carrageenase
EC 3.2.1.83
GH16 (Glycoside Hydrolase Family 16)
PF02368 (Big_2)
PF00722 (Glyco_hydro_16)
[Graphical View]

KEGG enzyme name
kappa-carrageenase
kappa-carrageenan 4-beta-D-glycanohydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P43478 CGKA_ALTCA Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans. Periplasm.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C02607 C00001 C04839
E.C.
Compound kappa-Carrageenan H2O 3-O-(3,6-Anhydro-alpha-D-galactopyranosyl)-D-galactose 4-O-sulfate
Type polysaccharide,sulfate group H2O polysaccharide,sulfate group
ChEBI 15377
PubChem 22247451
962
440506
1dypA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P43478 & literature [6]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dypA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 163;ASP 165;GLU 168

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.975
[6]
Fig.5, p.515-517, p.520 3

References
[1]
Resource
Comments
Medline ID
PubMed ID 2085807
Journal Carbohydr Res
Year 1990
Volume 208
Pages 127-38
Authors Piculell L, Rochas C
Title 87Rb+ spin relaxation in enzymically purified and in untreated iota-carrageenan.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1915370
Journal Eur J Biochem
Year 1991
Volume 201
Pages 241-7
Authors Potin P, Sanseau A, Le Gall Y, Rochas C, Kloareg B
Title Purification and characterization of a new kappa-carrageenase from a marine Cytophaga-like bacterium.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7737202
Journal Eur J Biochem
Year 1995
Volume 228
Pages 971-5
Authors Potin P, Richard C, Barbeyron T, Henrissat B, Gey C, Petillot Y, Forest E, Dideberg O, Rochas C, Kloareg B
Title Processing and hydrolytic mechanism of the cgkA-encoded kappa-carrageenase of Alteromonas carrageenovora.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10089334
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 918-20
Authors Michel G, Barbeyron T, Flament D, Vernet T, Kloareg B, Dideberg O
Title Expression, purification, crystallization and preliminary x-ray analysis of the kappa-carrageenase from Pseudoalteromonas carrageenovora.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11284500
Journal Carbohydr Res
Year 2001
Volume 331
Pages 101-6
Authors Knutsen SH, Sletmoen M, Kristensen T, Barbeyron T, Kloareg B, Potin P
Title A rapid method for the separation and analysis of carrageenan oligosaccharides released by iota- and kappa -carrageenase.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11435116
Journal Structure (Camb)
Year 2001
Volume 9
Pages 513-25
Authors Michel G, Chantalat L, Duee E, Barbeyron T, Henrissat B, Kloareg B, Dideberg O
Title The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases.
Related PDB 1dyp
Related UniProtKB

Comments
This enzyme belongs to the glycosidase family-16.

Created Updated
2004-03-22 2011-12-06