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P43478 (CGKA_PSEVC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Kappa-carrageenase

EC=3.2.1.83
Gene names
Name:cgkA
OrganismPseudoalteromonas carrageenovora (Alteromonas carrageenovora)
Taxonomic identifier227 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length397 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-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 16 family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkappa-carrageenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.1
Chain26 – 397372Kappa-carrageenase
PRO_0000011798

Sites

Active site1631Nucleophile
Active site1651
Active site1681Proton donor
Site2601Important for substrate recognition

Amino acid modifications

Disulfide bond98 ↔ 268

Secondary structure

...................................................... 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43478 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DA6D47C4682B10EF

FASTA39744,224
        10         20         30         40         50         60 
MKPISIVAFP IPAISMLLLS AVSQAASMQP PIAKPGETWI LQAKRSDEFN VKDATKWNFQ 

        70         80         90        100        110        120 
TENYGVWSWK NENATVSNGK LKLTTKRESH QRTFWDGCNQ QQVANYPLYY TSGVAKSRAT 

       130        140        150        160        170        180 
GNYGYYEARI KGASTFPGVS PAFWMYSTID RSLTKEGDVQ YSEIDVVELT QKSAVRESDH 

       190        200        210        220        230        240 
DLHNIVVKNG KPTWMRPGSF PQTNHNGYHL PFDPRNDFHT YGVNVTKDKI TWYVDGEIVG 

       250        260        270        280        290        300 
EKDNLYWHRQ MNLTLSQGLR APHTQWKCNQ FYPSANKSAE GFPTSMEVDY VRTWVKVGNN 

       310        320        330        340        350        360 
NSAPGEGQSC PNTFVAVNSV QLSAAKQTLR KGQSTTLEST VLPNCATNKK VIYSSSNKNV 

       370        380        390 
ATVNSAGVVK AKNKGTATIT VKTKNKGKID KLTIAVN 

« Hide

References

[1]"The gene encoding the kappa-carrageenase of Alteromonas carrageenovora is related to beta-1,3-1,4-glucanases."
Barbeyron T., Henrissat B., Kloareg B.
Gene 139:105-109(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-30 AND 33-37.
Strain: ATCC 43555 / DSM 6820 / IAM 12662 / NBRC 12985 / NCIMB 302.
[2]"The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases."
Michel G., Chantalat L., Duee E., Barbeyron T., Henrissat B., Kloareg B., Dideberg O.
Structure 9:513-525(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 27-297.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71620 Genomic DNA. Translation: CAA50624.1.
PIRI39507.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYPX-ray1.54A27-297[»]
ProteinModelPortalP43478.
SMRP43478. Positions 27-297.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16652.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR003343. Big_2.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
IPR008964. Invasin/intimin_cell_adhesion.
[Graphical view]
PfamPF02368. Big_2. 1 hit.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
SMARTSM00635. BID_2. 1 hit.
[Graphical view]
SUPFAMSSF49373. SSF49373. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43478.

Entry information

Entry nameCGKA_PSEVC
AccessionPrimary (citable) accession number: P43478
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 84 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries